76 results on '"John Biggins"'
Search Results
2. ‘Targeted Touchdown’ and ‘Partial Liftoff’: Post-Crisis Dispute Resolution in the OTC Derivatives Markets and the Challenge for ISDA*
- Author
-
John Biggins
- Subjects
050208 finance ,Standardization ,05 social sciences ,International economics ,Dispute resolution ,Boilerplate text ,ISDA Master Agreement ,0502 economics and business ,Derivatives market ,Sustenance ,Business ,050207 economics ,Notional amount ,Law ,Trade association - Abstract
Since the 1980s, influential participants in the niche over-the-counter (OTC) derivatives markets have sought to encourage contractual standardization in the industry to mitigate the potential for unforeseen legal interruptions and ensure the enforceability of OTC derivatives contracts. The International Swaps and Derivatives Association (ISDA), a trade association and standard-setter, has spearheaded this effort; resulting in the creation and sustenance of a highly successful transnational private regulatory regime (TPRER). Most notably, ISDA has generated a standardized boilerplate contract for OTC derivatives, known as the ‘ISDA Master Agreement’. However, the TPRER within which the ISDA Master Agreement operates displays some intriguing features and paradoxes. Chief amongst these paradoxes is that, while this TPRER appears at first glance to be highly legalistic and formal, indications are that rates of formal litigation between members of the regulatory regime have traditionally been low relative to the size of the market (the total notional amount of OTC derivatives contracts outstanding at the end of 2011 was estimated at US$648 trillion).
- Published
- 2012
3. Resolving the gaps: embedding ISDA in states’ responses to systemic risk
- Author
-
John Biggins and Colin Scott
- Subjects
Risk analysis (engineering) ,Systemic risk ,Embedding ,Business - Published
- 2016
4. Guest Editorial
- Author
-
Colin Scott and John Biggins
- Subjects
Political Science and International Relations ,Business and International Management ,Law - Published
- 2012
5. Public-Private Relations in a Transnational Private Regulatory Regime: ISDA, the State and OTC Derivatives Market Reform
- Author
-
John Biggins and Colin Scott
- Subjects
Finance ,European Union law ,business.industry ,media_common.quotation_subject ,State (polity) ,Political Science and International Relations ,Financial crisis ,Nation state ,Economics ,Derivatives market ,Business and International Management ,Element (criminal law) ,business ,Speculation ,Law ,Legitimacy ,Law and economics ,media_common - Abstract
It has frequently been claimed that over-the-counter (OTC) derivatives were, by and large, not directly regulated in the largest markets immediately prior to the global financial crisis (GFC). While there is an element of truth in this contention, it betrays the more complex interactions between public legislators and influential transnational private trade associations, most notably the International Swaps and Derivatives Association (ISDA), both prior to the GFC and in the wake of it. ISDA, its members and national governments interact on the basis of legal and policy tradeoffs which are ostensibly related to OTC derivatives’ regulatory treatment but which, in reality, extend beyond this. The fact of these interactions between ISDA and nation states may raise less regulatory legitimacy challenges than some of the norms which are communicated. A prime example is the public transposition of ‘safe harbours’ which insulate OTC derivatives, including ‘purely speculative’ contracts, from the full force of gambling law. It is thus suggested that while the regulatory role and expertise of ISDA should be formally recognised and appropriately harnessed by public actors in the creation of a new public-private regulatory detente in the OTC derivatives markets, a review of the appropriateness of the current legal treatment of purely speculative derivatives should be a priority for any such regulatory regime.
- Published
- 2012
6. Licensing the Gatekeeper? Public Pathways, Social Significance and the ISDA Credit Derivatives Determinations Committees
- Author
-
Colin Scott and John Biggins
- Subjects
Gatekeeping ,ISDA ,Corporate governance ,Financial market ,Regulatory reform ,Financial system ,Power (social and political) ,Shock (economics) ,Law ,Financial crisis ,Private governance ,Credit derivative ,Business ,Derivatives ,Regulation - Abstract
Regulatory relationships in financial markets exemplify the importance and changing nature of transnational business governance interactions (TBGI). These interactions involve reciprocal forces of influence between private and public regulators. We examine one key case of private governance in financial markets: the emergence, structures and decision-making of Credit Derivatives Determinations Committees (DCs) of the International Swaps and Derivatives Association (ISDA). We highlight the mechanisms or ‘pathways’ of interaction between ISDA, governments, courts and public regulators. We demonstrate how interactions between state and non-state actors can occur in both operational and policy spheres. We find ISDA to be a particularly resilient private regulator in an environment subject both to the significant external shock of the Global Financial Crisis and intense pressure on governmental actors to demonstrate that they are counteracting risk. We consider the sources of ISDA’s adaptive capacities. It is clear that ISDA operates as a key gatekeeper in the field and, significantly, the organisation appears to have a form of 'regulatory licensing' power in the DCs. This power of regulatory licence is derived in an immediate sense from the propagation of a web of contracts and norms established by market actors, the content of which is substantially derived from instruments such as the Master Agreement, set down by ISDA itself. But, equally importantly, we find that this regulatory licensing capacity is ultimately backstopped by an implicit delegation from public actors, which lends additional legitimacy to the DCs. Deposited by bulk import
- Published
- 2015
7. Protein−Protein Interactions between the Photosystem I Reaction Center Core and the PsaC Subunit
- Author
-
John Biggins and Hung-Cheng Chiou
- Subjects
Photosynthetic reaction centre ,Hydrophobic effect ,Crystallography ,Chemistry ,Ionic strength ,Protein subunit ,Mutant ,Materials Chemistry ,Biophysics ,Physical and Theoretical Chemistry ,Photosystem I ,Surfaces, Coatings and Films ,Protein–protein interaction - Abstract
The functional reconstitution of Photosystem I reaction center cores by wild-type and mutant PsaC subunits at high ionic strength indicated that hydrophobic interactions are dominant in stabilizing...
- Published
- 1998
8. Introduction of a [4Fe-4S (S-cys)4]+1,+2iron-sulfur center into a four-α helix protein using design parameters from the domain of the Fxcluster in the Photosystem I reaction center
- Author
-
Marvin Paul Scott and John Biggins
- Subjects
Photosynthetic reaction centre ,Crystallography ,Molecular model ,Ligand ,Chemistry ,Redox titration ,Helix ,Protein design ,Photosystem I ,Molecular Biology ,Biochemistry ,Cysteine - Abstract
We describe the insertion of an iron-sulfur center into a designed four alpha-helix model protein. The model protein was re-engineered by introducing four cysteine ligands required for the coordination of the mulinucleate cluster into positions in the main-chain directly analogous to the domain predicted to ligand the interpeptide [4Fe-4S (S-cys)4] cluster, Fx, from PsaA and PsaB of the Photosystem I reaction center. This was achieved by inserting the sequence, CDGPGRGGTC, which is conserved in PsaA and PsaB, into interhelical loops 1 and 3 of the four alpha-helix model. The holoprotein was characterized spectroscopically after insertion of the iron-sulfur center in vitro. EPR spectra confirmed the cluster is a [4Fe-4S] type, indicating that the cysteine thiolate ligands were positioned as designed. The midpoint potential of the iron-sulfur center in the model holoprotein was determined via redox titration and shown to be -422 mV (pH 8.3, n = 1). The results support proposals advanced for the structure of the domain of the [4Fe-4S] Fx cluster in Photosystem I based upon sequence predictions and molecular modeling. We suggest that the lower potential of the Fx cluster is most likely due to factors in the protein environment of Fx rather than the identity of the residues proximal to the coordinating ligands.
- Published
- 1997
9. Dirty complexity: money laundering through derivatives
- Author
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John Biggins
- Subjects
Public economics ,Economics ,Monetary economics ,Money laundering - Published
- 2013
10. Private Governance, Public Implications and the Tightrope of Regulatory Reform: The ISDA Credit Derivatives Determinations Committees
- Author
-
Colin Scott and John Biggins
- Subjects
business.industry ,Corporate governance ,media_common.quotation_subject ,Financial market ,Financial system ,Accounting ,Regulatory reform ,Private governance ,Shock (economics) ,State (polity) ,Financial crisis ,Credit derivative ,Business ,media_common - Abstract
Regulatory relationships in financial markets exemplify the importance and changing nature of transnational business governance interactions (TBGI). These interactions involve reciprocal forces of influence between private and public regulators. This paper examines one key case of private governance in financial markets: the emergence, structures and decision-making of Credit Derivatives Determinations Committees (DCs) of the International Swaps and Derivatives Association (ISDA). The paper highlights the mechanisms or ‘pathways’ of interaction between ISDA, governments, courts and public regulators. Interactions between state and non-state actors are shown to occur in both operational and policy spheres. ISDA is found to be a particularly resilient private regulator in an environment subject both to the significant external shock of the global financial crisis and intense pressure on governmental actors to demonstrate that they are counteracting risk. The reasons behind ISDA’s adaptive capacities are considered.
- Published
- 2013
11. Site-Directed Mutagenesis of the Subunit PsaC Establishes a Surface-Exposed Domain Interacting with the Photosystem I Core Binding Site
- Author
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John Biggins, Suzanne M. Rodday, Harry A. Frank, Veeradej Chynwat, and Lien T. Do
- Subjects
Light ,Protein subunit ,Molecular Sequence Data ,Photosynthetic Reaction Center Complex Proteins ,Mutant ,Arginine ,Cyanobacteria ,Photosystem I ,Biochemistry ,Electron transfer ,Spinacia oleracea ,Amino Acid Sequence ,Binding site ,Site-directed mutagenesis ,DNA Primers ,Alanine ,Binding Sites ,P700 ,Base Sequence ,Photosystem I Protein Complex ,Chemistry ,Electron Spin Resonance Spectroscopy ,Membrane Proteins ,Proteins ,Kinetics ,Crystallography ,Mutagenesis, Site-Directed ,Biophysics - Abstract
We have postulated that the orientation of PsaC on the photosystem I core involves electrostatic interactions between charged residues on the core binding site and the subunit [Rodday, S. M., Jun, S.-S., & Biggins, J. (1993) Photosynth. Res. 36, 1-9]. We, therefore, changed eight acidic residues on PsaC to arginine and examined the efficiency of the mutant subunits in the reconstitution of P700-Fx cores in vitro. Reconstitution of the cores by the mutant subunits was determined by analysis of the kinetics of recombination reactions between P700+ and reduced acceptors as measured optically. Restoration of complete forward electron transfer, indicative of efficient subunit binding, was estimated from the ca. 30 ms decay component in the flash transients. Slightly reduced levels of reconstitution were observed for the mutants D24R, E46R/D47R. D61R, and E72R. In contrast, mutants D9R, E27R, and D32R showed significantly lower efficiencies. The presence of the iron-sulfur centers, FA and FB, in these three mutant subunits was confirmed by low-temperature EPR spectroscopy indicating that the polypeptides had folded correctly. We conclude that the introduction of positively charged side chains at positions 9, 27, and 32 seriously disrupts PsaC binding. However, when the wild-type acidic residues in these positions were changed to alanine, only mutant D9A showed a reduced level of reconstitution, suggesting that this aspartate is the most important residue participating in the electrostatic interaction with the core. The results are discussed in relation to the photosystem I crystal structure and support an orientation of PsaC on the core such that center FB is proximal to Fx.
- Published
- 1996
12. Evidence That the FX Domain in Photosystem I Interacts with the Subunit PsaC: Site-Directed Changes in PsaB Destabilize the Subunit Interaction in Chlamydomonas reinhardtii
- Author
-
John Biggins, Andrew N. Webber, Suzanne M. Rodday, and Scott E. Bingham
- Subjects
Photosynthetic reaction centre ,Chloroplasts ,Macromolecular Substances ,Stereochemistry ,Protein subunit ,Molecular Sequence Data ,Photosynthetic Reaction Center Complex Proteins ,Mutant ,Chlamydomonas reinhardtii ,Ligands ,Photosystem I ,Biochemistry ,Electron Transport ,Structure-Activity Relationship ,Bacterial Proteins ,Animals ,Amino Acid Sequence ,Photosynthesis ,Peptide sequence ,DNA Primers ,Photosystem ,Base Sequence ,Photosystem I Protein Complex ,biology ,Chemistry ,Mutagenesis ,Membrane Proteins ,biology.organism_classification ,Mutagenesis, Site-Directed ,Oxidation-Reduction ,Protein Binding - Abstract
The highly conserved amino acid sequence PCDGPGRGGTC in both photosystem I reaction center core proteins PsaA and PsaB has been predicted to contribute the four cysteine ligands for coordination of the 4Fe-4S iron-sulfur cluster FX, and we have proposed a working model for the binding of PsaC to this domain of the reaction center core heterodimer [Rodday et al. (1993) Photosynth. Res. 36, 1-9]. We have investigated structure-function relationships between this domain and the PsaC subunit by site-directed mutagenesis of the conserved prolines P560 and P564, and the charged residues D562 and R566 in the eucaryotic alga Chlamydomonas reinhardtii. The D562N and R566E mutants did not accumulate the PsaA and PsaB reaction center proteins, indicating that these residues are essential for the stable assembly of photosystem I. The P560A, P560L, and P564L mutants accumulated functional reaction centers but showed an impaired interaction between the reaction center core complex and the PsaC subunit. We observed that the reaction centers of the proline mutants dissociated more readily in urea, and reconstitution of the mutant core preparations using PsaC and Fe-S cluster insertion protocols in vitro were incomplete. We suggest that P560 and D562 contribute to the stability of the FX cluster, most likely by providing essential hydrogen bonding to the C561 ligand. The data obtained from the P564 and R566 replacements provide direct evidence that the intercysteinyl region in PsaB is a domain involved in the interaction between PsaC and the reaction center core.
- Published
- 1995
13. The Implementation of the Services Directive in Ireland
- Author
-
John Biggins and Catherine M Donnelly
- Subjects
Judicial review ,Political science ,Corporate governance ,Law ,Wish ,media_common.cataloged_instance ,Transposition (logic) ,European union ,Directive ,media_common ,Law library - Abstract
John Biggins, BA, LL.M (Dub)—Research Associate, Centre for Regulation and Governance, University College Dublin. Catherine Donnelly, LL.B. (Dub)—B.C.L. (Oxon); LL.M. (Harv); D.Phil. (Oxon); Barrister, Blackstone Chambers, London, Law Library, Dublin; Attorney at Law, New York; Lecturer in Law, Trinity College, Dublin., latest update July 2011.The authors wish to thank the Department of Jobs, Enterprise and Innovation for helpful guidance regarding the transposition of the SD in Ireland. The views expressed herein are the authors’ alone and do not necessarily represent the views of any other individual or organisation. Errors and omissions also remain the authors’ alone.
- Published
- 2012
14. Extending and Contracting Jurisdictions in a Transnational Private Regulatory Regime: Efficiency, Legitimacy, ISDA and the OTC Derivatives Markets
- Author
-
Colin Scott and John Biggins
- Subjects
State (polity) ,media_common.quotation_subject ,Financial crisis ,Nation state ,Derivatives market ,Business ,Element (criminal law) ,Speculation ,Legitimacy ,Law and economics ,media_common - Abstract
It has frequently been claimed that over-the-counter (OTC) derivatives were, by and large, not directly regulated in the largest markets immediately prior to the global financial crisis (GFC). While there is an element of truth in this contention, it betrays the more complex interactions between public legislators and influential transnational private trade associations, most notably the International Swaps and Derivatives Association (ISDA), both prior to the GFC and in the wake of it. ISDA, its members and national governments interact on the basis of legal and policy tradeoffs which are ostensibly related to OTC derivatives' regulatory treatment but which, in reality, extend beyond this. The fact of these interactions between ISDA and nation states may raise less regulatory legitimacy challenges than some of the norms which are communicated. A prime example is the public transposition of ‘safe harbours’ which insulate OTC derivatives, including ‘purely speculative’ contracts, from the full force of gambling law. It is thus suggested that while the regulatory role and expertise of ISDA should be formally recognised and appropriately harnessed by public actors in the creation of a new public-private regulatory detente in the OTC derivatives markets, a review of the appropriateness of the current legal treatment of purely speculative derivatives should be a priority for any such regulatory regime.
- Published
- 2011
15. Salt-dependent protein phosphorylation in the cyanobacteriumSynechocystisPCC 6803
- Author
-
Dortje Golldack, Norbert Erdmann, Martin Hagemann, and John Biggins
- Subjects
biology ,Osmotic shock ,Synechocystis ,biology.organism_classification ,Microbiology ,Biochemistry ,In vivo ,Labelling ,Genetics ,Phosphorylation ,Protein phosphorylation ,Signal transduction ,Protein kinase A ,Molecular Biology - Abstract
Hyper- and hypo-osmotic salt shocks in the presence of [32P]PO43− led to the appearance and disappearance of several 32P-labelled proteins in vivo within a few minutes. Similar to the in vivo labelling experiments, a 20.5-kDa protein was also more intensely labelled in extracts from salt-shocked cells using [γ-32P]ATP in in vitro labelling experiments. Furthermore, labelling of this and a protein of about 64.4 kDa was induced by adding high amounts of NaCl directly to extracts of control cells in kinase assays. Therefore, changes in the NaCl contents led to alterations of the activity of protein in Synechocystis sp. PCC 6803, which may be involved in the signal transduction chain sensing changes in the NaCl content of the surrounding medium.
- Published
- 1993
16. Interaction of the FAFB-containing subunit with the Photosystem 1 core heterodimer
- Author
-
Suzanne M. Rodday, Sung-Soo Jun, and John Biggins
- Subjects
Phenylglyoxal ,Arginine ,Chemistry ,Stereochemistry ,Protein subunit ,Iron–sulfur cluster ,macromolecular substances ,Cell Biology ,Plant Science ,General Medicine ,Trypsin ,Photosystem I ,Biochemistry ,Electron transfer ,chemistry.chemical_compound ,medicine ,Peptide sequence ,medicine.drug - Abstract
The structure of the predicted amino acid sequence in the FX domain of Photosystem 1 was studied by molecular modeling and a working hypothesis was developed for the functional interaction of PsaC with the core heterodimer. We propose that the intervening sequences between homologous cysteines in the FX cluster form two flexible loops and participate in the binding of PsaC, and that the arginine residues in the two surface-exposed loops may promote the interaction between the P700-FX core and the subunit. The model was tested experimentally; chemical modification of arginine residues in the P700-FX core using phenylglyoxal prevented reconstitution of the core with PsaC and PsaD after insertion of FeS clusters in vitro. Treatment of the P700-FX core with trypsin also prevented reconstitution of terminal electron transfer to FAFB, although neither treatments affected the electron transfer to FX as judged by flash kinetic spectrophotometry. Electron transfer in the P700-FAFB complex was not impaired by either phenylglyoxal or trypsin treatment indicating that the small subunit(s) protect the arginine residues that become chemically modified or cleaved. The data are consistent with the working model and point to additional experiments designed to identify the specific residues involved in the interaction between the P700-FX core and PsaC.
- Published
- 1993
17. Reconstitution and exchange of quinones in the A1 site of Photosystem I. An electron spin polarization electron paramagnetic resonance study
- Author
-
Seth W. Snyder, John Biggins, Marion C. Thurnauer, Richard R Rustandi, and James R. Norris
- Subjects
chemistry.chemical_classification ,Biophysics ,Analytical chemistry ,Cell Biology ,Photochemistry ,Photosystem I ,Biochemistry ,Acceptor ,Benzoquinone ,Naphthoquinone ,Quinone ,law.invention ,chemistry.chemical_compound ,Electron transfer ,chemistry ,law ,Electron paramagnetic resonance ,Alkyl - Abstract
The electron spin polarized (ESP) electron paramagnetic resonance (EPR) signal observed in spinach Photosystem I (PS I) particles was examined in preparations depleted of vitamin K 1 by solvent extraction, followed by reconstitution with a series of quinones and quinone analogues. The ESP EPR signal was previously attributed to a radicalpair that included vitaim K 1 − (Rustandi, R.R., et al. (1990) Biochemistry 29, 8030–8032) and, in addition, vitamin K 1 was assigned as the secondary acceptor A 1 in PS I (Snyder, S.W., et al. (1991) Proc. Natl. Acad. Sci. USA, 88, 9895–9896). The ESP EPR signal was observed in untreated PS I preparations, was not detected in the solvent-extracted PS I samples and was restored upon reconstitution using certain quinones. The ability to restore the ESP EPR signal was dependent upon two properties of the reconstituted acceptor. First, the solution reduction potential of the reconstituted acceptor must be more positive than about −750 mV where the solution reduction potential of vitamin K 1 is −710 mV. Second, the structure of the reconstituted acceptor requires either a minimum of two aromatic rings (i.e., naphthoquinone) or a benzoquinone (or larger) derivative substituted with an alkyl tail. A model was developed to describe both the requirements for electron transfer to A 1 and also previous results for electron transfer from A 1 − to the iron-sulfur centers (Biggins, J. (1990) Biochemistry 29, 7259–7264). When untreated PS I preparations were incubated with perdeuterated vitamin K 1 (DK 1 ) the endogenous K 1 was observed to exchange with DK 1 . The replacement rate was strongly dependent upon temperature (h-days at 4°C, min at 37°C) and upon illumination (min). Naphthoquinones lacking a long alkyl tail were unable to exchange with endogenous vitamin K 1 . Although no known physiological role exists for vitamin K 1 ejection from its A 1 binding site, the quinone appears to be somewhat labile. Direct exchange of vitamin K 1 with exogenously supplied quinones indicates that the PS I A 1 site might be a target for the design of new herbicides in green plants.
- Published
- 1992
18. Fluorescence studies of photoregulation in the chrysophyte Ochromonas danica
- Author
-
Robert S. Knox, Pam B. Gibbs, Robert H. Hwang-Schweitzer, and John Biggins
- Subjects
Photosystem II ,Chemistry ,Biophysics ,General Chemistry ,Condensed Matter Physics ,Photosystem I ,Biochemistry ,Fluorescence ,Atomic and Molecular Physics, and Optics ,Ochromonas danica ,Decay curve ,Amplitude ,Atomic physics ,Excitation ,Photosystem - Abstract
Three physiological states brought about by different preillumination conditions in Ochromonas danica (state 1, state 2, and dark adapted) have been investigated using steady-state and time-resolved fluorescence at 77 K. The former reveals that the photosystem 1 (PS1) emission amplitude is the same in states 1 and 2. The photosystem 2 (PS2) emission amplitude depends on preillumination, state 1 having a higher peak than state 2 and dark adapted cells. Emission decay curves from PS1 are independent of preillumination, while decay curves from PS2 are identical for state-2 and dark adapted cells (1/e time 310 ps), state 1 showing a slower decay (1/e time 390 ps). No evidence suggests a preillumination-dependent redistribution of excitation energy from PS2 to PS1. Variation in the amplitude of a long-lifetime component appears to be sufficient to explain the state-dependent changes in emission of the PS2 peak. This is consistent with the hypothesis that some peripheral antenna is energetically decoupling without redistributing the excitation energy upon the state 2 to state 1 transition, causing increased emission in the 670–700 nm region.
- Published
- 1992
19. Thylakoid Organization in the Chromophyte Alga Ochromonas danica
- Author
-
John Biggins and Pamela B. Gibbs
- Subjects
Gel electrophoresis ,Chlorophyll a ,Chromatography ,Physiology ,Sodium ,chemistry.chemical_element ,Plant Science ,Biology ,chemistry.chemical_compound ,Pigment ,chemistry ,Biochemistry ,Chlorophyll ,Thylakoid ,visual_art ,Genetics ,visual_art.visual_art_medium ,Lauryldimethylamine oxide ,Chlorophyll fluorescence - Abstract
This report describes the isolation and preliminary characterization of a new pigment-protein complex from the chromophyte alga, Ochromonas danica. The pigment-protein complex was obtained by extracting a thylakoid membrane preparation with the zwitterionic detergent lauryldimethylamine oxide followed by ultracentrifugation on sucrose gradients. The pigment-protein complex has been characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, absorption spectroscopy, and low temperature (77 Kelvin) chlorophyll fluorescence spectroscopy. A polypeptide with a monomeric molecular weight of 31,000 as determined by denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis was the major constituent of this pigment-protein complex. The major pigment in this complex was chlorophyll a, although an as yet unidentified carotenoid was also present. There was no evidence for the presence of chlorophyll c.
- Published
- 1991
20. In Vivo and In Vitro Protein Phosphorylation Studies on Ochromonas danica, an Alga with a Chlorophyll a/c/Fucoxanthin Binding Protein
- Author
-
Pamela B. Gibbs and John Biggins
- Subjects
Photosystem II ,Physiology ,Binding protein ,macromolecular substances ,Plant Science ,Biology ,Photosystem I ,environment and public health ,Biochemistry ,Thylakoid ,Genetics ,Protein phosphorylation ,Kinase activity ,Protein kinase A ,Photosystem - Abstract
The phosphorylation of thylakoid membranes in the Chromophyte alga Ochromonas danica was studied in whole cells and in vitro. Protein kinase activity was observed in the thylakoid fraction, and several membrane-bound polypeptides were found to be phosphorylated. The thylakoid protein kinase demonstrated several unusual regulatory properties. Both the polypeptides that were phosphorylated and the rate of protein phosphorylation were independent of illumination. Protein kinase activity was also unaffected by 3-(3,4-dichlorophenyl)-1,1-dimethylurea, diuron. The kinase activity was inhibited under strong reducing conditions. Whole cells labeled with (32)PO(4) (3-) were converted to light states I and II by pre-illumination favoring photosystem I or photosystem II, respectively. Analysis of the phosphoproteins from cells in state I and state II showed that no changes in phosphorylation accompanied the change in energy redistribution.
- Published
- 1991
21. Prototype Decision Support System for Analyzing Impact of Catchment Policies
- Author
-
J. Richard Davis, Peter Laut, John Biggins, and Paul M. Nanninga
- Subjects
Government ,Engineering ,Decision support system ,Land use ,Operations research ,business.industry ,Suite ,media_common.quotation_subject ,Geography, Planning and Development ,Environmental resource management ,Water supply ,Management, Monitoring, Policy and Law ,Water resources ,Local government ,Quality (business) ,business ,Water Science and Technology ,Civil and Structural Engineering ,media_common - Abstract
The South Australian government has recently formed a committee to investigate conflicts over the use of resources in the Mt. Lofty Ranges, including improvements to the quality of water supplied to the city of Adelaide. The committee is examining potential land-use and land-management policies. The writers have developed a prototype of a decision support system (DSS) that will estimate the effects of these policies on water quality and the costs of implementing the policies. The DSS consists of three modules. The policy module allows the user to build up a suite of policies in a formal syntax. The second module, the catchment model, will estimate the effects of these policies on total phosphorus, total nitrogen, and turbidity levels. The user can query the DSS about these estimates in the third module. The prototype has been evaluated by the South Australian Engineering and Water Supply Department, and a second version of the DSS is now being designed.
- Published
- 1991
22. Evaluation of selected benzoquinones, naphthoquinones, and anthraquinones as replacements for phylloquinone in the A1 acceptor site of the photosystem I reaction center
- Author
-
John Biggins
- Subjects
chemistry.chemical_classification ,Photosynthetic reaction centre ,Binding Sites ,Photosystem I Protein Complex ,Photosynthetic Reaction Center Complex Proteins ,Anthraquinones ,Vitamin K 1 ,Electron acceptor ,Photochemistry ,Photosystem I ,Biochemistry ,Electron transport chain ,Acceptor ,Quinone ,Electron Transport ,Electron transfer ,chemistry.chemical_compound ,chemistry ,Benzoquinones ,Oxidation-Reduction ,Naphthoquinones - Abstract
Selected substituted 1,4-benzoquinones, 1,4-naphthoquinones, and 9,10-anthraquinones were investigated as possible replacement quinones in spinach photosystem I (PSI) preparations that had been depleted of endogenous phylloquinone by extraction with hexane/methanol. As a criterion for successful biochemical reconstitution, the restoration of electron transfer was determined by measuring P-430 turnover at room temperature from flash-induced absorbance transients. Restoration of complete electron transfer between A0- and P-430 (terminal iron-sulfur centers, FAFB) was demonstrated by using phylloquinone, 2-methyl-3-decyl-1,4-naphthoquinone, 2-methyl-3-(isoprenyl)2-1,4-naphthoquinone, and 2-methyl-3-(isoprenyl)4-1,4-naphthoquinone. All other quinones tested did not restore P-430 turnover but acted as electron acceptors and oxidized A0-. It is concluded that the specificity of the replacement quinone for interaction with the primary acceptor, A0-, is low but additional structural constraints are required for the quinone occupying the A1 site to donate to the iron-sulfur center, Fx. It is suggested that the 3-phytyl side chain of phylloquinone and the 3-alkyl tails of the three naphthoquinones that restored P-430 turnover may be required for interaction with a hydrophobic domain of the A1 site in the PSI core to promote electron transfer to Fx and then to FAFB.
- Published
- 1990
23. Contribution of vitamin K1 to the electron spin polarization in spinach photosystem I
- Author
-
John Biggins, T. J. Michalski, Richard R. Rustandi, Marion C. Thurnauer, L. L. Feezel, James R. Norris, and Seth W. Snyder
- Subjects
P700 ,Photosystem I Protein Complex ,biology ,Photochemistry ,Chemistry ,Photosynthetic Reaction Center Complex Proteins ,Electron Spin Resonance Spectroscopy ,Resonance ,Vitamin K 1 ,biochemical phenomena, metabolism, and nutrition ,Photosystem I ,biology.organism_classification ,Biochemistry ,Redox ,Quinone ,law.invention ,Electron Transport ,Electron transfer ,fluids and secretions ,law ,Spinach ,Electron paramagnetic resonance ,Oxidation-Reduction - Abstract
The electron spin polarized (ESP) electron paramagnetic resonance (EPR) signal observed in spinach photosystem I (PSI) particles was examined in preparations depleted of vitamin K1 by solvent extraction and following biological reconstitution by the quinone. The ESP EPR signal was not detected in the solvent-extracted PSI sample but was restored upon reconstitution with either protonated or deuterated vitamin K1 under conditions that also restored electron transfer to the terminal PSI acceptors. Reconstitution using deuterated vitamin K1 resulted in a line narrowing of the ESP EPR signal, supporting the conclusion that the ESP EPR signals in the reconstituted samples arise from a radical pair consisting of the oxidized PSI primary donor, P700+, and reduced vitamin K1.
- Published
- 1990
24. Tomorrow the World : In Which Cadet Otto Prohaska Carries the Habsburg Empire's Civilizing Mission to the Entirely Unrece
- Author
-
John Biggins and John Biggins
- Subjects
- Historical fiction, Sea stories, War stories, World War, 1914-1918--Naval operations, Austrian, World War, 1914-1918--Africa--Fiction
- Abstract
Laced with smart humor, this naval tale follows the early career of Lieutenant Otto Prohaska, a cadet in the Austro - Hungarian Navy at the turn of the century. Bad luck continues to shadow Otto, and when a fellow cadet breaks his leg, Otto must take his place on a scientific expedition bound for disaster. But even sinister quack scientists, a misguided attempt to establish a colony in Africa, and angry South Sea cannibals bent on destruction cannot keep Otto from fulfilling his patriotic duty.
- Published
- 2007
25. Tomorrow the World : In Which Cadet Otto Prohaska Carries the Habsburg Empire's Civilizing Mission to the Entirely Unreceptive People of Africa and Oceania
- Author
-
John Biggins and John Biggins
- Abstract
Laced with smart humor, this naval tale follows the early career of Lieutenant Otto Prohaska, a cadet in the Austro–Hungarian Navy at the turn of the century. Bad luck continues to shadow Otto, and when a fellow cadet breaks his leg, Otto must take his place on a scientific expedition bound for disaster. But even sinister quack scientists, a misguided attempt to establish a colony in Africa, and angry South Sea cannibals bent on destruction cannot keep Otto from fulfilling his patriotic duty.
- Published
- 2007
26. Structure-function studies on the interaction of PsaC with the Photosystem 1 heterodimer : The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803
- Author
-
L. Mclntosh, R. Schulz, Suzanne M. Rodday, and John Biggins
- Subjects
chemistry.chemical_classification ,Photosynthetic reaction centre ,Protein subunit ,Mutant ,Wild type ,Cell Biology ,Plant Science ,General Medicine ,Photosystem I ,Biochemistry ,Divalent ,chemistry ,Biophysics ,Binding site ,Site-directed mutagenesis - Abstract
The interaction of PsaC with the core heterodimer of Photosystem 1 was studied in wild type Synechocystis sp. PCC 6803 and the site-directed mutant R561E of PsaB. The mutant reaction center was much less stable in urea and the functional reconstitution of the mutant core using PsaC was impaired. However, the extent of reconstitution increased in the presence of divalent cations whereas that of the wild type was inhibited. We conclude that the reaction center in the mutant is unstable, most likely due to the introduction of an unfavorable electrostatic interaction between surface-exposed residues on PsaC and the binding site for the subunit on the core heterodimer in support of the model proposed previously (Rodday et al. (1993) Photosynth Res 36: 1–9).
- Published
- 1994
27. Photosynthetic electron-transfer reactions in the green sulfur bacterium Chlorobium vibrioforme: evidence for the functional involvement of iron-sulfur redox centers on the acceptor side of the reaction center
- Author
-
Seth W. Snyder, Xingmin Liu, John Biggins, Mette Miller, and Marion C. Thurnauer
- Subjects
Photosynthetic reaction centre ,Iron-Sulfur Proteins ,Photosynthetic Reaction Center Complex Proteins ,Iron–sulfur cluster ,Chlorosome ,Chlorobium ,Photochemistry ,Biochemistry ,Redox ,Electron Transport ,chemistry.chemical_compound ,Electron transfer ,Photosynthesis ,biology ,Bacteria ,Cell Membrane ,Electron Spin Resonance Spectroscopy ,Temperature ,biology.organism_classification ,Electron transport chain ,Acceptor ,Kinetics ,chemistry ,Spectrophotometry ,Oxidation-Reduction ,NADP - Abstract
The green sulfur bacterium Chlorobium vibrioforme was cultured in the presence of ethylene to selectively inhibit the synthesis of the chlorosome antenna BChl d. Use of these cells as starting material simplified the isolation of a photoactive antenna-depleted membrane fraction without the use of high concentrations of detergents. The preparation had a BChl alpha/P840 of 50, and the spectral properties were similar to those of preparations isolated from cells grown with a normal complement of chlorosomes. The membrane preparation was active in NADP+ photoreduction. This indicated that the fraction contained reaction centers with complete electron-transfer sequences which were then characterized further by flash kinetic spectrophotometry and EPR. We confirmed that cytochrome c553 is the endogenous donor to P840+, and at room temperature we observed a recombination reaction between the reduced terminal acceptor and P840+ with a t1/2 = 7 ms. Oxidative degradation of iron-sulfur centers using low concentrations of chaotropic salts introduced a faster recombination reaction of t1/2 = 50 microseconds which was lost at higher concentrations of chaotrope, indicating the participation of another iron-sulfur redox center earlier than the terminal acceptor. Cluster insertion using ferric chloride and sodium sulfide in the presence of 2-mercaptoethanol restored both the 50-microseconds and 7-ms recombination reactions, allowing definitive assignments of these centers as iron-sulfur centers. Following the suggestion of Nitschke et al. [(1990) Biochemistry 29, 3834-3842], we associate these two kinetic phases to back-reactions between P840+ and iron-sulfur centers FX and FAFB, respectively. The iron-sulfur cluster degradation and reconstitution protocols also led to inhibition and restoration of NADP+ photoreduction by the membrane preparation, providing unequivocal evidence for the function of the centers FX and FAFB in the physiological electron-transfer sequence on the acceptor side of the Chlorobium reaction center. At 77 K we observed a recombination reaction of t1/2 = 20 ms that we suggest occurs between Fx- and P840+. Degradation of the iron-sulfur clusters resulted in replacement of the 20-ms phase with a faster reaction of t1/2 = 80 microseconds that was most likely a recombination between the early acceptor A1- and P840+ or decay of 3P840. Analysis of the iron-sulfur centers in the preparation by EPR at cryogenic temperature supports the optical measurements. EPR signals originating from the terminal acceptor(s) were not observed following treatment of the membrane preparation by chaotropes, and a modified signal was restored following cluster reinsertion.(ABSTRACT TRUNCATED AT 400 WORDS)
- Published
- 1992
28. Direct assignment of vitamin K1 as the secondary acceptor A1 in photosystem I
- Author
-
James R. Norris, John Biggins, Marion C. Thurnauer, Seth W. Snyder, and Richard R. Rustandi
- Subjects
chemistry.chemical_classification ,Multidisciplinary ,Chemistry ,Radical ,Analytical chemistry ,Electron acceptor ,Photochemistry ,Resonance (chemistry) ,Photosystem I ,Acceptor ,Quinone ,law.invention ,Electron transfer ,law ,Electron paramagnetic resonance ,Research Article - Abstract
The characteristic electron spin polarized electron paramagnetic resonance (ESP EPR) signal observed in photosystem I (PSI) has been previously assigned to a radical pair composed of the oxidized primary donor and a reduced vitamin K1. Under conditions in which Bottin, H. & Setif, P. [(1991), Biochim. Biophys. Acta 105, 331-336] proposed that A1 is doubly reduced, the ESP EPR signal was not observed. Therefore, the ESP EPR signal can be directly attributed to A-1, and vitamin K1 can be assigned as this PSI acceptor. The ESP EPR signal was partially restored by removal of the chemical reductants.
- Published
- 1991
29. The Two-Headed Eagle : In Which Otto Prohaska Takes a Break As the Habsburg Empire's Leading U-boat Ace and Does Something Even More Thanklessly Dangerous
- Author
-
John Biggins and John Biggins
- Subjects
- World War, 1914-1918--Italy--Fiction, World War, 1914-1918--Aerial operations, Austrian--Fiction
- Abstract
It is the summer of 1916 and, as luck would have it, Otto is assigned to the nascent, unreliable, and utterly frightening Imperial and Royal Austro-Hungarian Flying Service. Ottto's aerial chauffeur is the self-willed Sergeant-Pilot Toth, with whom he can only communicate in broken Latin—although when all else fails, screaming will suffice! On the ground the rickety Habsburg Empire begins to crumble before the onslaught of WWI, while in the air Otto confronts a series of misadventures and the winds of change.
- Published
- 2006
30. The Emperor's Coloured Coat : In Which Otto Prohaska, Hero of the Habsburg Empire, Has an Interesting Time While Not Quite Managing
- Author
-
John Biggins and John Biggins
- Subjects
- World War, 1914-1918--Naval operations, Austrian--Fiction
- Abstract
This book follows the hapless Lieutenant Otto Prohaska in the waning years of the Austro-Hungarian Empire and finds Otto taking an ill-considered break from duties to engage in a mad fling with a Polish actress. After a desperate attempt to elude his lover's husband, he finds himself mistaken by anarchists as one of their own. Otto soon masters their code names and secret handshakes, but when he also learns of their plans to assassinate the Archduke Ferdinand in Sarajevo, his duty is clear. He must alert his superiors—now, if only he can find someone who will believe him!
- Published
- 2006
31. Functional Role of Phylloquinone on the Acceptor Side of Photosystem 1
- Author
-
Normand A. Tanguay, John Biggins, and Harry A. Frank
- Subjects
Functional role ,P700 ,biology ,Chemistry ,Photosystem I ,biology.organism_classification ,Photochemistry ,Acceptor ,Redox ,law.invention ,Quinone ,law ,Spinach ,Electron paramagnetic resonance - Abstract
The stabilization of charge in the primary reaction of PSI is promoted by rapid electron transfer reactions involving the five redox centers A0A1FxFAFB (1). A0 is monomelic Chl a and FxFAFB are 4Fe:4S clusters. FX is associated with the PSI core and FAFB are localized on an 8·9 kDa polypeptide. Provisional identification of A1 as a quinone was based upon the EPR signal of A1 (2,3) and comparison of the electron spin polarized flash-induced EPR K-band spectrum of the species P700+A1 - with that of P870 +Q- in Fe-depleted bacterial reaction centers (4). Direct support for the participation of quinone followed a study of flash-induced optical transients at low temperature (5) and the specific reconstitution of room temperature electron transfer reactions in solvent-extracted cyanobacterial PSI using phylloquinone (vitamin K1) (6). The reconstitution studies have been recently confirmed using an ether-extracted preparation of PSI derived from spinach (7).
- Published
- 1990
32. Thylakoid Protein Phosphorylation in an Algae with Chlorophyll A/C/Fucoxanthin Light Harvesting Antenna
- Author
-
John Biggins and Pamela B. Gibbs
- Subjects
Cyanobacteria ,biology ,Light-harvesting complexes of green plants ,macromolecular substances ,Photosynthesis ,biology.organism_classification ,chemistry.chemical_compound ,Peridinin ,chemistry ,Algae ,Biophysics ,Fucoxanthin ,Phycobilin ,sense organs ,Chlorophyll fluorescence - Abstract
Mechanisms for the regulation of excitation energy distribution between PS2 and PS1 have been proposed for higher plants (mobile antenna hypothesis) and for red algae cyanobacteria (spillover). These organisms utilize Chl b and phycobilins respectively as accessory light harvesting pigments. The Chromophytic algae encompass a taxonomically diverse group of phyla which are very successful competitors and contribute substantially to net global photosynthesis. These algae are characterized by their use of Chl c and carotenoid (fucoxanthin or peridinin) as accessory light harvesting pigments and by the arrangement of their thylakoids into extended bands of three. Despite their obvious importance, there has only been one prior report on the regulation of energy transfer in Chromophytic algae in which Owens (1) reported only intensity dependent changes. We have previously shown that the Chromophyte Ochromonas danica shows wavelength dependent changes in chlorophyll fluorescence (both 77K and room temperature) which are diagnostic for a re-distribution of excitation energy (2). We report here on the antenna polypeptide composition of O. danica as well as the in vitro protein kinase activity.
- Published
- 1990
33. A Sailor of Austria : In Which, Without Really Intending To, Otto Prohaska Becomes Official War Hero No. 27 of the Habsburg
- Author
-
John Biggins and John Biggins
- Subjects
- World War, 1914-1918--Naval operations, Austrian--Fiction
- Abstract
In this ironic, hilarious, and poignant story, Otto Prohaska is a submarine captain serving the almost-landlocked Austro-Hungarian Empire. He faces a host of unlikely circumstances, from petrol poisoning to exploding lavatories to trigger-happy Turks. All signs point to the total collapse of the bloated empire he serves, but Otto refuses to abandon the Habsburgs in their hour of need.
- Published
- 2005
34. Mechanism of the light state transition in photosynthesis. I. Analysis of the kinetics of cytochrome f oxidation in State 1 and State 2 in the red alga, Porphyridium cruentum
- Author
-
John Biggins
- Subjects
Cytochrome f ,Cytochrome ,biology ,Chemistry ,Biophysics ,DCMU ,macromolecular substances ,Cell Biology ,Photosynthesis ,Photochemistry ,biology.organism_classification ,Biochemistry ,Electron transport chain ,chemistry.chemical_compound ,Porphyridium cruentum ,biology.protein ,Phycobilisome ,Photosystem - Abstract
The kinetics of photooxidation and reduction of cytochrome f were examined spectrophotometrically in the red alga Porphyridium cruentum in light State 1 and light State 2. Experiments were performed on intact cells that had been chemically fixed and stabilized in the light states. The cytochrome f turnover was measured during conditions of linear electron transport driven by both photosystems and during several cyclic reactions mediated by the long-wavelength Photosystem (PS) I. The data show that the rate of photooxidation of cytochrome f increased in State 2 when the cells were activated by subsaturating intensities of green light absorbed primarily by the phycobilisome. No differences in kinetics were found between algae in State 1 or State 2 when they were activated by light absorbed primarily by the chlorophyll of PS I. The results confirm that changes in energy distribution between the two photosystems occur as a result of the light state transition and verify that the redistribution of excitation results in the predicted changes in electron transport.
- Published
- 1983
35. Excitation-energy redistribution in the cryptomonad alga Cryptomonas ovata
- Author
-
Ursula K. Snyder and John Biggins
- Subjects
Electron transfer ,Photosystem II ,Chemistry ,Excited state ,Biophysics ,Photophosphorylation ,Cell Biology ,Photochemistry ,Photosynthesis ,Photosystem I ,Biochemistry ,Fluorescence ,Photosystem - Abstract
We have studied the redistribution of excitation energy in the cryptomonad alga Cryptomonas ovata . Low-temperature fluorescence emission spectra from cells preilluminated with light 1 and light 2 show that preferential excitation of Photosystem II (PS II) leads to decreased fluorescence emission from chlorophyll (Chl) a associated with PS II relative to the emission following the preferential excitation of Photosystem I (PS I). The fluorescence change is indicative of a light-state transition by the cells. However, comparision of measurements of the kinetics of P-700 photooxidation by cells fixed with glutaraldehyde following illumination with light 1 or light 2 shows that the relative activity of PS I is lower in cells fixed in light 2. This is in contrast to the expectation for cells in State 2. Excitation spectra for the fluorescence emission from PS II Chl a show that preferential excitation of PS II leads to a decreased probability for energy transfer from phycoerythrin and Chl c 2 to PS II when compared to cells in which PS I is preferentially excited. This result is in accordance with recent picosecond time-resolved fluorescence studies (Bruce, D., Biggins, J., Charbonneau, S. and Thewalt, M. (1987) in Progress in Photosynthesis Research (Biggins, J., ed.), Vol. II, pp. 777–780, Martinus Nijhoff, Dordrecht) and we, therefore, suggest that C. ovata does not undergo a classical light-state transition. However, preferential excitation of PS II or PS I appears to cause pigment-protein conformational changes which change the probability for energy transfer from phycoerythrin to PS II, and we suggest that this may be a mechanism for photoprotection of PS II. Studies of the kinetics of excitation-energy redistribution, and of the effects of electron-transport inhibitors and uncouplers of photophosphorylation indicate that the mechanism for excitation-energy redistribution in C. ovata and phycobilisome-containing organisms may be similar.
- Published
- 1987
36. Energy distribution in the photochemical apparatus of Porphyridium cruentum: Picosecond fluorescence spectroscopy of cells in state 1 and state 2 at 77 K
- Author
-
Doug Bruce, John Biggins, Lucia E. Hancock, Cheryl A. Hanzlik, and Robert S. Knox
- Subjects
Allophycocyanin ,Photosystem II ,biology ,Chemistry ,Cell Biology ,Plant Science ,General Medicine ,Photochemistry ,biology.organism_classification ,Biochemistry ,Fluorescence ,Fluorescence spectroscopy ,Porphyridium cruentum ,Phycocyanin ,Emission spectrum ,Photosystem - Abstract
Excitation energy distribution in Porphyridium cruentum in state 1 and state 2 was investigated by time resolved 77 K fluorescence emission spectroscopy. The fluorescence rise times of phycoerythrin, phycocyanin and allophycocyanin (in cells in state 1 and state 2) were very similar in contrast to the emission from chlorophyll a (Chl a) associated with the two photosystems. In state 2 photosystem II (PSII) Chl a fluorescence emission rose faster than the PSI Chl a emission and decayed more rapidly, and the converse was observed in state 1. These kinetic data support the concept of increased energy transfer from PSII Chl a to PSI Chl a in state 2 in P. cruentum.
- Published
- 1986
37. Role of cyclic electron transport in photosynthesis as measured by the photoinduced turnover of P700 in vivo
- Author
-
John Biggins and Peter C. Maxwell
- Subjects
P700 ,Light ,Photosystem II ,Chemistry ,Eukaryota ,Plastoquinone ,macromolecular substances ,Photosystem I ,Photochemistry ,Photosynthesis ,Biochemistry ,Electron transport chain ,Electron Transport ,Kinetics ,chemistry.chemical_compound ,Species Specificity ,Spectrophotometry ,Mutation ,Cytochromes ,Plastocyanin ,Photosystem - Abstract
The light-induced turnover of P700 was measured spectrophotometrically in a wide variety of algae and some photosynthetic mutants. Analysis of the postillumination recovery of P700+ revealed that the apparent first-order rate constant for reduction via the cyclic pathway was much lower that that via the noncyclic pathway. After activation of photosystems 1 and 2 the half-time for reduction of P700+ was 5-20 ms, whereas after activation of primarily photosystem 1 a longer half-time of ca. 150 ms was observed. The extent of the photooxidation of P700 was the same in both regimes of illumination. The longer half-time was also noted after inhibition of photosystem 2 by 3-(3,4-dichlorophenyl)-1,1-dimethylurea or mild heat shock and in mutant algae known to lack a functional photosystem 2. No signal was observed in mutants lacking P700 itself but those strains lacking either plastocyanin or cytochrome f were capable of a very slow turnover (reduction t 1/2 greater than 500 ms at room temperature). This very slow turnover was not affected by carbonyl cyanide m-chlorophenylhydrazone or the plastoquinone antagonist, 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone, indicating that the pathway for reduction of P700+ in these mutants is not energy linked and does not utilize the intersystem electron transport chain. The slow, 150 ms, reduction of P700+ due to cyclic flow was not observed when cells were engaged in photosynthesis at high-light intensities. The data are interpreted as evidence for the involvement of the total functional pool of P700 in both electron transport pathways, and we suggest that cyclic electron transport does not contribute to photosynthesis in oxygen-evolving autotrophs.
- Published
- 1976
38. EXCITATION ENERGY TRANSFER IN THE CRYPTOPHYTES. FLUORESCENCE EXCITATION SPECTRA AND PICOSECOND TIME-RESOLVED EMISSION SPECTRA OF INTACT ALGAE AT 77 K
- Author
-
John Biggins, Mike L. W. Thewalt, T. Steiner, and Doug Bruce
- Subjects
Photosystem II ,biology ,Phycobiliprotein ,Analytical chemistry ,General Medicine ,Chroomonas ,Photochemistry ,Photosystem I ,biology.organism_classification ,Biochemistry ,Fluorescence ,Phycocyanin ,biology.protein ,Emission spectrum ,Physical and Theoretical Chemistry ,Phycoerythrin - Abstract
Excitation spectra of chlorophyll-a (Chl-a) fluorescence in intact cells of Cryptomonas ovata, Chroomonas pauciplastida and Chroomonas salina were determined at 77 K. For all species the excitation spectra for emission from Chl-a associated with photosystem II (PSII) showed increased contributions by a carotenoid (493 nm) and phycobiliproteins, and decreased contributions by carotenoid (417 nm, 505 nm) and Chl-a (445 nm) as compared to excitation spectra for emission from Chl-a associated with photosystem I (PSI). Excitation spectra of C. salina and C. ovata showed an increased contribution by Chl-c2 to PSII Chl-a fluorescence emission. In all three species the absorbance band positions of Chl-a, as determined from the excitation spectra, were similar to those previously described in green plants. green algae and phycobilisome-containing organisms. Time-resolved 77 K fluorescence emission spectra of C. ovata and C. salina showed successive emission from both phycoerythrin and Chl-c2, PSII Chl-a, and PSI Chl-a. C. pauciplastida showed successive emission from phycocyanin, PSII Chl-a, and PSI Chl-a. Spectral red-shifts with time were observed for the phycobiliprotein peaks in all three species. The fluorescence decay of phycoerythrin in C. ovata and C. salina was faster than that of phycocyanin in C. pauciplastida. The results are discussed in relation to the organization of the antenna pigments of PSII and PSI in the cryptophyte algae.
- Published
- 1986
39. Electron transfer reactions in photosystem I following vitamin K1 depletion by ultraviolet irradiation
- Author
-
Normand A. Tanguay, Harry A. Frank, and John Biggins
- Subjects
Photosystem I ,Chlorophyll ,Vitamin ,Vitamin K ,Photochemistry ,Ultraviolet Rays ,Ultraviolet irradiation ,Photosynthetic Reaction Center Complex Proteins ,Light-Harvesting Protein Complexes ,Biophysics ,Photosynthesis ,Biochemistry ,Electron Transport ,chemistry.chemical_compound ,Electron transfer ,Structural Biology ,Genetics ,Molecular Biology ,Plant Proteins ,Photosystem ,P700 ,Photosystem I Protein Complex ,Vitamin K1 ,Electron Spin Resonance Spectroscopy ,Primary reaction ,Vitamin K 1 ,Cell Biology ,Optical transient ,Acceptor ,Quinone ,chemistry ,EPR ,Oxidation-Reduction ,NADP - Abstract
Photosystem I preparations were irradiated with UV to destroy vitamin K1 in situ. The depletion of vitamin K1 resulted in inactivation of NADP+ photoreduction and introduction of a approximately 220 ms component in the flash generated P700+ rereduction at room temperature. The photoreduction of the terminal FeS centers FA and FB in control and vitamin K1-depleted preparations at 7 K were comparable. The data confirm that vitamin K1 is functionally implicated in primary electron transfer reactions in PS I at physiological temperature, and that the anomalous results at cryogenic temperature may be explicable in terms of a by-pass of the vitamin K1 acceptor site or heterogeneity introduced into the photosystem by quinone removal.
- Published
- 1989
40. Mechanism of the light-state transition in photosynthesis
- Author
-
Doug Bruce and John Biggins
- Subjects
Allophycocyanin ,Chemistry ,Biophysics ,Analytical chemistry ,Context (language use) ,Cell Biology ,Dichroism ,Photochemistry ,Linear dichroism ,Biochemistry ,Thylakoid ,Phycocyanin ,Phycobilisome ,Photosystem - Abstract
Linear-dichroism spectra of Anacystis nidulans at 77 K were determined for whole cells chemically fixed in light State 1 and light State 2. Whole cells were oriented by the squeezed gel technique using 5% gelatin 2.2 M sucrose gels. Peaks with positive dichroism were observed at 638 nm and 688 nm with shoulders at approx. 650 nm and 700 nm. The amplitude of the 650 nm shoulder was greater for cells in State 2 than those in State 1, and the State-2-minus-State 1 difference spectrum had a single peak at 656 nm. The linear dichroism spectrum of phycobilisomes isolated from A. nidulans showed peaks at 635 nm (phycocyanin) and 656 nm (allophycocyanin). The spectrum for thylakoid membranes free of phycobilisomes had one peak at 685 nm with a shoulder at 698 nm. We suggest that the change in dichroism at 656 nm between cells in State 1 and State 2 results from a change in orientation of the allophycocyanin core of the phycobilisome. This result is discussed in the context of our model for the light-state transition in phycobilisome-containing organisms.
- Published
- 1985
41. Performance characteristics of an electronically tunable acousto‐optic filter for fast scanning spectrophotometry
- Author
-
John Biggins, Charles W. Wade, and William S. Shipp
- Subjects
Materials science ,business.industry ,Stray light ,Bandwidth (signal processing) ,Grating ,law.invention ,Wavelength ,Optics ,law ,Modulation ,Contrast ratio ,Monochromatic color ,business ,Instrumentation ,Monochromator - Abstract
A commercially available CaMoO4 tunable acousto‐optic filter has been evaluated for use as a monochromator and modulator for incorporation into a rapid scanning spectrophotometer for the wavelength range 450–750 nm. The construction of a suitable rf driver is described. The bandwidth of light transmitted by the filter was found to be between 2 and 6 A, permitting excellent spectral resolution. The contrast ratio was greater than 1400 over the major portion of the tuning range, and the skirt rejection was 35–40 dB for 1‐nm‐wide bands 10–100 nm distant from the center wavelength. The transmission of the filter can be switched in 20 μsec, and modulation frequencies up to 25 kHz are attainable without appreciable loss of transmission. With a conventional light source the output intensity of monochromatic light is comparable to grating monochromators. Stray light can be effectively compensated for by transmission modulation and phase‐sensitive detection of the output. We show that the use of the filter as a monochromator is in many respects superior to the other devices which have been used previously for rapid scanning. The filter may also be used as a light modulator or multiple‐beam spectrophotometer and, by virture of its electronic control and ease of interfacing with digital computers, can be considered to be a programmable light source.
- Published
- 1976
42. Regulation of the distribution of excitation energy in Ochromonas danica, an organism containing a chlorophyll-A/C/carotenoid light harvesting antenna
- Author
-
John Biggins and Pamela B. Gibbs
- Subjects
Chlorophyll a ,DCMU ,Cell Biology ,Plant Science ,General Medicine ,Photochemistry ,Biochemistry ,Fluorescence ,Light-harvesting complex ,chemistry.chemical_compound ,Light intensity ,chemistry ,Emission spectrum ,Chlorophyll fluorescence ,Photosystem - Abstract
A chlorophyll a, c-fucoxanthin pigment-protein complex8 functions as the major light harvesting antenna in the Chrysophyte Ochromonas danica. The regulated distribution of excitation energy between the two photosystems was investigated in these organisms and was shown to be strongly wavelength dependent. A light state transition was induced by pre-illumination of cells using light 2 (640 nm) and light 1 (700 nm) of equal absorbed intensity, and detected by reversible changes in the 77 K chlorophyll fluorescence emission spectra. Peaks at ∼ 690 nm and ∼ 720 nm in the low temperature spectra are most likely associated with PS2 and PS1 respectively. A room temperature fluorescence emission at 680 nm induced by modulated light 2 (500 nm) was strongly quenched in the presence of background light 1 (720 nm). Removal of light 1 led to an increase in fluorescence followed by a slow quenching. The room temperature fluorescence changes were directly correlated with changes in the 77 K emission spectra that indicated a change in the distribution of excitation energy between the two photosystems. It was established that DCMU (1 μmol) prevented the state 2. The conversion to state 1 followed a simple photochemical dose dependence and had a half-time of 20 s-1.5 min at 6 W m(-2). In contrast, the conversion to state 2 was independent of light intensity. These data indicate that O. danica undergoes a light state transition in response to the preferential excitation of PS2 or PS1.
- Published
- 1989
43. The kinetic behavior of P-700 during the induction of photosynthesis in algae
- Author
-
John Biggins and Peter C. Maxwell
- Subjects
Bacteria ,Light ,Photosystem II ,Chemistry ,Oscillation ,Kinetics ,Biophysics ,Eukaryota ,DCMU ,Cell Biology ,Darkness ,Photosystem I ,Photochemistry ,Photosynthesis ,Biochemistry ,Redox ,chemistry.chemical_compound ,Cytochromes ,Oxidation-Reduction ,Photosystem - Abstract
The kinetics of P -700 were examined spectrophotometrically during the induction of photosynthesis in algae. A pronounced oscillation was observed in the redox level of P -700 upon illumination of dark-adapted cells. The dark adaptation required approximately 1 min. The oscillation may be described as an initial rapid oxidation reaching a peak at approx. 50 ms followed by complete reduction of the pool of P -700. A subsequent slower oxidation resulted in attainment of the final state around 1 s. The main features of the oscillation were qualitatively the same in a wide variety of algae. The modulation in redox level of P -700 required high intensity activation of both photosystems and was eliminated by pre-illumination of the cells with weak short wavelength light but not by longer wavelengths absorbed primarily by Photosystem I. We propose that the P -700 modulation is directly related to the fast redox changes in Photosystem II which occur during the induction of photosynthesis. Cells incubated with methyl viologen did not show the P -700 oscillation confirming the suggestion previously advanced that exhaustion of Photosystem I acceptor and kinetic limitations in the carbon reduction cycle partially control the fast phase of photosynthetic induction.
- Published
- 1977
44. Functional role of vitamin K1 in photosystem I of the cyanobacterium Synechocystis 6803
- Author
-
Paul Mathis and John Biggins
- Subjects
chemistry.chemical_classification ,Vitamin ,Photosynthetic reaction centre ,biology ,Stereochemistry ,Kinetics ,Synechocystis ,Electron acceptor ,Photosystem I ,biology.organism_classification ,Photochemistry ,Biochemistry ,Acceptor ,Electron transfer ,chemistry.chemical_compound ,chemistry - Abstract
The function of vitamin K1 in the primary electron-transfer processes of photosystem I (PS I) was investigated in the cyanobacterium Synechocystis 6803. A preparation of purified PS I was found to contain two vitamin K1's per reaction center. One vitamin K1 was removed by extraction with hexane, and further extraction using hexane including 0.3% methanol resulted in a preparation devoid of vitamin K1. The hexane-extracted PS I was functional in the photoreduction of NADP+, but the PS I after extraction using hexane-methanol was totally inactive. Activity was restored by using exogenous vitamin K1 plus the hexane extract. Vitamin K3 would not substitute. The room temperature recombination kinetics of the PS I extracted with hexane were not significantly modified. However, following the removal of both vitamin K1's, the 20-ms recombination between P-700+ and P-430- was replaced by a dominant relaxation (t 1/2 = 30 ns) due to recombination of the primary biradical P-700+ A0- and a slower component originating from the P-700 triplet. This kinetic behavior was consistent with an interruption of forward electron transfer to the acceptor A1. Addition of either vitamin K1 or vitamin K3 to such preparations resulted in restoration of the slow kinetic phase (greater than 2 ms), indicating significant competition by the two exogenous quinones for electron transfer from A0-. In the case of vitamin K3, this change in the kinetics induced by vitamin K1, suggesting successful reconstitution of the acceptor site A1. These data support the hypothesis that acceptor A1 is vitamin K1 and is a component of the electron-transfer pathway for NADP+ reduction.
- Published
- 1988
45. Thylakoid conformational changes accompanying membrane protein phosphorylation
- Author
-
John Biggins
- Subjects
Conformational change ,Chemistry ,Biophysics ,food and beverages ,Plastoquinone ,macromolecular substances ,Cell Biology ,Photochemistry ,Linear dichroism ,environment and public health ,Biochemistry ,chemistry.chemical_compound ,Membrane ,Thylakoid ,Phosphorylation ,Protein phosphorylation ,sense organs ,skin and connective tissue diseases ,Photosystem - Abstract
The effect of reversible membrane phosphorylation on the room temperature linear dichroism signal of magneto-oriented pea thylakoids was investigated. Membrane phosphorylation, induced by photoreduction of the plastoquinone pool, resulted in a change in the linear dichroism signal in the region of the red absorption band of chlorophyll. The optical change was due to modifications in selective polarized light scattering which have been shown to be indicative of alterations in the degree of membrane stacking. No changes in linear dichroism due to a reorientation of pigments were observed. It is concluded that phosphorylation of the membrane results in about a 10% destacking of the thylakoids and that this conformational change is implicated in energy redistribution between the two photosystems.
- Published
- 1982
46. Mechanism of the light state transition in photosynthesis. II. Analysis of phosphorylated polypeptides in the red alga, Porphyridium cruentum
- Author
-
John Biggins, Christine L. Campbell, and Doug Bruce
- Subjects
Gel electrophoresis ,Biophysics ,Cell Biology ,Biology ,biology.organism_classification ,Biochemistry ,Fluorescence ,Fluorescence spectroscopy ,Porphyridium cruentum ,Phycobilisome ,Protein phosphorylation ,Chlorophyll fluorescence ,Photosystem - Abstract
The possible involvement of a reversible protein phosphorylation event in the regulation of excitation energy distribution was studied in the red alga Porphyridium cruentum. Whole cells were incubated in phosphate-depleted growth medium containing carrier-free [32P]orthophosphate for several hours to label the intracellular phosphate pools, and they were then converted to State 1 or State 2 by illumination using blue or green light, respectively. The successful transition to State 1 or State 2 was verified by 77 K fluorescence spectroscopy of the chlorophyll emission and the cells were then denatured using either acetone, trichloroacetic acid or boiling detergent. The whole cell lysates were solubilized, treated with RNAase, and analyzed for phosphoproteins by SDS-polyacrylamide gel electrophoresis. At least twelve polypeptides were found to be phosphorylated but no changes in specific radioactivity of the polypeptides were detected when samples from cells in State 1 and State 2 were compared. We conclude that a reversible protein phosphorylation event is not implicated in the state transition in P. cruentum. A model is presented for the mechanism of the light state transition in organisms that contain phycobilisomes which is different from the mechanism of energy distribution proposed for higher plants.
- Published
- 1984
47. CO2 Assimilation by Etiolated Hordeum vulgare Seedlings during the Onset of Photosynthesis
- Author
-
Roderic B. Park and John Biggins
- Subjects
Physiology ,Chemistry ,Botany ,Etiolation ,Genetics ,Assimilation (biology) ,Plant Science ,Hordeum vulgare ,Autotroph ,Photosynthesis - Abstract
The assimilation of CO 2 by etiolated Hordeum vulgare seedlings during an illumination period indicates a conversion of the organisms to autotrophy. After 1 hour illumination, increases in the photo-assimilation of CO 2 are observed and the distribution of C 14 in the soluble fraction of the plants is predominantly in intermediates of the Calvin cycle.
- Published
- 1966
48. Respiratory Mechanisms in the Flexibacteriaceae: Terminal Oxidase Systems of Saprospira grandis and Vitreoscilla Species
- Author
-
John Biggins and William E. Dietrich
- Subjects
Cytochrome ,Physiology and Metabolism ,Antimycin A ,Centrifugation ,Ascorbic Acid ,Vibration ,Microbiology ,Electron Transport ,chemistry.chemical_compound ,Oxygen Consumption ,Molecular Biology ,Carbon Monoxide ,Oxidase test ,Cyanides ,Bacteria ,Cell-Free System ,biology ,Succinate dehydrogenase ,Cell Membrane ,Succinates ,Hydrogen-Ion Concentration ,NAD ,biology.organism_classification ,Ascorbic acid ,Electron transport chain ,Culture Media ,Succinate Dehydrogenase ,Peroxidases ,Biochemistry ,chemistry ,Spectrophotometry ,biology.protein ,Cytochromes ,Vitreoscilla ,Oxidoreductases ,Oxidation-Reduction ,Protein Binding ,Peroxidase - Abstract
Particles from both Saprospira grandis and Vitreoscilla species, obtained by high-pressure extrusion and sonic treatment, respectively, actively catalyze the oxidation of reduced nicotinamide adenine dinucleotide (NADH) and succinate with O 2 . These activities are inhibited by cyanide but not by antimycin; Saprospira is also amytal- and rotenone-insensitive. Vitreoscilla preparations were unable to oxidize mammalian ferrocytochrome c and reduced tetramethyl- p -phenylenediamine, whereas the Saprospira preparations did so actively. Low-temperature (77 K) difference spectroscopy of Vitreoscilla cells and particles indicates the presence of three maxima in the cytochrome alpha-region at 554, 558, and 562 nm. All three cytochromes are active in NADH and succinate oxidation, but none is ascorbate reducible. Cytochrome o is the only CO-binding pigment present and is probably the terminal oxidase; it has properties similar to the cytochrome o isolated in solubilized form from this organism. Saprospira cells and membranes exhibit four cytochrome absorption bands whose maxima are at 550, 554, 558, and 603 nm at 77 K. The latter component has not been noted previously. NADH and succinate reduce all four cytochromes, but ascorbate reduces only the 550- and 603-nm pigments. CO spectra indicate the presence of cytochrome a,a 3 which is probably the oxidase. A second CO-binding pigment is present which is not a peroxidase but may be a cytochrome.
- Published
- 1971
49. Photo-induced electron paramagnetic resonance in mutant photosynthetic species lacking carotenoids or chlorophyll
- Author
-
John Biggins, M.F. Singleton, G.M. Androes, and Melvin Calvin
- Subjects
Chlorophyll ,Hepatophyta ,chemistry.chemical_classification ,Light ,biology ,Mutant ,Electron Spin Resonance Spectroscopy ,Eukaryota ,Light-harvesting complexes of green plants ,General Medicine ,Chlorobium ,Photosynthesis ,biology.organism_classification ,Photochemistry ,Carotenoids ,law.invention ,chemistry.chemical_compound ,chemistry ,law ,Electron paramagnetic resonance ,Carotenoid - Abstract
The association of the photo-induced electron paramagnetic resonance signal in photosynthetic tissue with the necessity for the presence of chlorophyll is demonstrated with a variety of mutant organisms. This is taken as additional evidence of the direct electron-transfer reaction from and/or to chlorophyll as the primary quantum conversion step.
- Published
- 1963
50. Respiratory mechanisms in the Flexibacteriaceae
- Author
-
William E. Dietrich and John Biggins
- Subjects
Mucor ,Cytochrome ,biology ,Cytochrome b ,Cyanide ,Cytochrome c ,Biophysics ,Antimycin A ,Oxidative phosphorylation ,biology.organism_classification ,Biochemistry ,chemistry.chemical_compound ,chemistry ,biology.protein ,Ferricyanide ,Molecular Biology - Abstract
Membrane fragments from the marine flexibacterium Leucothrix mucor can be obtained by disrupting the cells by sonication or high-pressure extrusion. Such preparations are active in the oxidation of NADH and succinate and are inhibited by antimycin A, HOQNO, cyanide, and CO. The antimycin inhibition can be bypassed by TMPD. NADH-oxidase is not inhibited by rotenone or amytal. The particles can also interact in oxidative activities with DPIP, PMS, ferricyanide, ascorbate, and mammalian cytochrome c . Low-temperature (−196 °) difference spectrophotometry of whole cells and particles reveals the presence of four absorption bands in the α region of cytochromes, the relative absorbencies of which are markedly affected by growth conditions of the cells. From observations on the steady-state level of reduction of these components in the presence of various substrates, reductants, and inhibitors, we propose that the sequence of electron carriers is: substrate→ B 562 → C 552(458) → B 558 → oxygen. The only CO-binding pigment present in this organism is photodissociable at room temperature but not at −196 ° and is spectroscopically similar to cytochrome o . We suggest that this pigment is the functional terminal oxidase in L. mucor and is equivalent to cytochrome B 558 .
- Published
- 1968
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