23 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
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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. Guest Editorial
- Author
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Colin Scott and John Biggins
- Subjects
Political Science and International Relations ,Business and International Management ,Law - Published
- 2012
4. Licensing the Gatekeeper? Public Pathways, Social Significance and the ISDA Credit Derivatives Determinations Committees
- Author
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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
5. Protein−Protein Interactions between the Photosystem I Reaction Center Core and the PsaC Subunit
- Author
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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
6. 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
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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
7. Private Governance, Public Implications and the Tightrope of Regulatory Reform: The ISDA Credit Derivatives Determinations Committees
- Author
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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
8. Fluorescence studies of photoregulation in the chrysophyte Ochromonas danica
- Author
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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
9. Thylakoid Organization in the Chromophyte Alga Ochromonas danica
- Author
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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
10. In Vivo and In Vitro Protein Phosphorylation Studies on Ochromonas danica, an Alga with a Chlorophyll a/c/Fucoxanthin Binding Protein
- Author
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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
11. Direct assignment of vitamin K1 as the secondary acceptor A1 in photosystem I
- Author
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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
12. Electron transfer reactions in photosystem I following vitamin K1 depletion by ultraviolet irradiation
- Author
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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
13. CO2 Assimilation by Etiolated Hordeum vulgare Seedlings during the Onset of Photosynthesis
- Author
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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
14. Respiratory Mechanisms in the Flexibacteriaceae: Terminal Oxidase Systems of Saprospira grandis and Vitreoscilla Species
- Author
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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
15. Reorientation of a long-wavelength chlorophyll-a—protein by divalent cations as revealed by the linear dichroism of magneto-oriented thylakoids
- Author
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Jan Svejkovský and John Biggins
- Subjects
chemistry.chemical_classification ,Chlorophyll a ,Chemistry ,Biophysics ,Analytical chemistry ,Cell Biology ,Photochemistry ,Linear dichroism ,Biochemistry ,Divalent ,chemistry.chemical_compound ,Long wavelength ,Structural Biology ,Thylakoid ,Genetics ,Molecular Biology ,Magneto - Full Text
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16. The role of plastoquinone in the in vivo photosynthetic cyclic electron transport pathway in algae
- Author
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John Biggins
- Subjects
Time Factors ,Light ,Biophysics ,Plastoquinone ,Chlorella ,Acetates ,Photosynthesis ,Biochemistry ,Plastid terminal oxidase ,Electron Transport ,chemistry.chemical_compound ,Algae ,Species Specificity ,Structural Biology ,In vivo ,Genetics ,Carbon Radioisotopes ,Molecular Biology ,Lighting ,Plant Proteins ,biology ,Chemistry ,Quinones ,Oxidation reduction ,Cell Biology ,Darkness ,biology.organism_classification ,Electron transport chain ,Kinetics ,Glucose ,Spectrophotometry ,Diuron ,Rhodophyta ,Cytochromes ,Electron Transport Pathway ,Oxidation-Reduction - Published
- 1974
17. Physical Properties of Spinach Chloroplast Lamellar Proteins
- Author
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John Biggins and Roderic B. Park
- Subjects
Physiology ,Chemistry ,Fraction (chemistry) ,Plant Science ,Articles ,Photosynthesis ,Electron transport chain ,Chloroplast ,chemistry.chemical_compound ,Membrane ,Biochemistry ,Chlorophyll ,Botany ,Genetics ,Photosynthetic membrane ,Chemical composition - Abstract
The chlorophyll-containing lamellae within higher plant chloroplasts are the site of the light reactions and associated electron transport reactions of the photosynthetic process (12, 19). Investigations on the chemical composition of purified spinach chloroplast lamellae have shown that they are about 50 % protein and 50 % lipid (13). Of the 2 fractions, the lipid has been studied the most extensively owing to the considerable interest in the photosynthetic pigments. and the majority of the fraction can be accounted for by known compounds (8, 11). The protein fraction contains the 2 cytochromes, f anid b,; and the transitioln metals iron (nonheme), manigalnese and copper (13). This fraction has received very little direct attention, presumably owing to the extreme insolubility of the material at phvsiological pH and the lack of appropriate enzymological tools to cope with the problem. Davenport and Hill (3) purified cytochromle f from an ammoniacal ethanolic extract of fresh parsley leaves by ammonium sulfate fractionation and calcium phosphate gel adsorption. The pure protein was shown to be MW = 110,000 and contained 2 hemes. Indirect evidence concerning the properties of the protein fraction comes from work primarily designed to investigate the nature of the chlorophyll-protein link in attempts to elucidate the state of chlorophyll in vivo (14,15). For this purpose a wide variety of detergents and organic solvents have been used to solubilize the membranes of chloroplasts. It was decided that a similar use of detergents for the removal of lipid from the lamelflae and solubilizationi of the protein would be a fruitful approach to the studv of the chloroplast protein fraction. These methods have also been shown to be of great value in the study of the mitochonidrion where similar problems of protein insolubility prevail (5). This report describes the preparation and some physical properties of the protein fraction of chlloroplast lamellae in an attempt to derive informiiationl pertinent to the molecular architecture of the photosynthetic membrane.
- Published
- 1965
18. Photosynthetic Reactions by Lysed Protoplasts and Particle Preparations from the Blue-Green Alga, Phormidium luridum
- Author
-
John Biggins
- Subjects
Lysis ,Chromatography ,Cytochrome ,Physiology ,Cytochrome b ,Cytochrome c ,Photophosphorylation ,Plant Science ,Articles ,Biology ,Electron transport chain ,Membrane ,Genetics ,biology.protein ,Plastocyanin - Abstract
Reactions of photosynthetic electron transport and photophosphorylation were studied in preparations from the blue-green alga, Phormidium luridum. Osmotic lysis of protoplasts proved to be a superior technique for the production of cell-free preparations with high enzymatic activity. Such lysed protoplasts sustain high rates of photophosphorylation coupled to the photo-reduction of NADP(+) or ferricyanide. P/2e(-) ratios close to unity were routinely observed. The same preparations, and also those prepared by grinding the cells in solutions containing sucrose or ethylene glycol, are active in cyclic photophosphorylation mediated by phenazine methosulfate or dichloro-phenolindophenol. The particles prepared by grinding the cells are, however, inactive in non-cyclic photophosphorylation.Extensive washing of the membranes with solutions containing sucrose removes the majority of the residual soluble fraction of the algal cell which includes cytochromes C(554) and C(549) and phycocyanin. Cyclic photophosphorylation activity is unimpaired by this treatment, but is abolished when the membranes are washed with very dilute buffers. This activity is restored by the addition of a soluble protein which is not a known redox constituent such as cytochrome C(554) or plastocyanin, and may be a coupling factor.Analysis of the well-washed membranes by low temperature (77 degrees K) difference spectrophotometry reveals the presence of cytochrome b(6) and a bound form of cytochrome C(554) in proportions similar to that found in higher plant chloroplasts. The concentration of the membrane-bound cytochrome C(554), relative to cytochrome b(6) is not altered by extensive washing, sonication or treatment with 1% digitonin. This indicates that this cytochrome is an integral component of the cytoplasmic lamellae and we suggest that it is of functional significance. The soluble form of cytochrome C(554), which is present in concentrations about 3-fold higher than the bound form, depending upon growth conditions, is not essential for cyclic photophosphorylation. The concentration of cytochrome b(6): chlorophyll a was found to be 1:500.Under the conditions employed, we were unable to detect a bound form of the low potential cytochrome C(549).
- Published
- 1967
19. Respiration in blue-green algae
- Author
-
John Biggins
- Subjects
Adenosine monophosphate ,Microbial Physiology and Metabolism ,Eukaryota ,Oxidative phosphorylation ,Biology ,Nicotinamide adenine dinucleotide ,NAD ,Microbiology ,Electron transport chain ,Oxidative Phosphorylation ,Electron Transport ,chemistry.chemical_compound ,Adenosine diphosphate ,Adenosine Triphosphate ,Oxygen Consumption ,chemistry ,Biochemistry ,NAD+ kinase ,Molecular Biology ,Adenosine triphosphate ,Nicotinamide adenine dinucleotide phosphate ,NADP - Abstract
The low rate of endogenous respiration exhibited by the blue-green algae Anacystis nidulans and Phormidium luridum was not increased by the addition of respiratory substrates. However, endogenous respiration was inhibited by low concentrations of cyanide and by high carbon monoxide tensions. In addition, the uncouplers dinitrophenol and carbonyl cyanide p -trifluoromethoxyphenylhydrazone both stimulated the respiratory rate. The transition of cells from the aerobic steady state to anaerobiosis was accompanied by a decrease in the concentration of cellular nicotinamide adenine dinucleotide phosphate (NADP + ) and adenosine triphosphate (ATP), whereas the concentration of nicotinamide adenine dinucleotide (NAD + ) was unchanged. Concomitant with the metabolite decreases were stoichiometric increases io reduced NADP + (NADPH), adenosine diphosphate, and adenosine monophosphate. A decrease in ATP was also observed after the addition of uncouplers. These data are interpreted as evidence for the association of oxidative phosphorylation with the oxidation of NADP + -linked substrates in these algae. Membrane fragments isolated from the algal cells oxidized succinate, malate, ferrocytochrome c , ascorbate-tetramethyl- p -phenylenediamine, and reduced 2,6-dichlorophenol indophenol but did not oxidize NADPH or reduced NAD + in a cyanide-sensitive system. Oxidative phosphorylation has not yet been demonstrated in these fragments, but a dark ATP-P i exchange, distinct from the lighttriggered exchange associated with photosynthesis, is readily observed. This exchange was inhibited by phloridzin, Atabrine, and uncouplers in concentrations which suggest that the mechanism of oxidative phosphorylation in blue-green algae is different from that found in other bacteria and in mitochondria. These results led to the conclusion that the biochemical basis for obligate autotrophy in these organisms does not lie in the metabolic events associated with terminal electron transport and energy conservation.
- Published
- 1969
20. Quantasome: Size and Composition
- Author
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John Biggins and Roderic B. Park
- Subjects
Crystallography ,Chlorophyll content ,chemistry.chemical_compound ,Multidisciplinary ,chemistry ,Volume (thermodynamics) ,Chlorophyll ,Quantasome ,chemistry.chemical_element ,Molecule ,Composition (visual arts) ,Manganese - Abstract
The quantasome as seen in a two-dimensional crystalline array is 185 A long, 155 A wide, and 100 A thick. The surface of the quantasome appears to contain four or more subunits. The molecular weight, determined from volume and density measurements, is 2 x 10(6) This is twice the minimum molecular weight calculated from the manganese content and corresponds to a chlorophyll content of 230 chlorophyll molecules per quantasome.
- Published
- 1964
21. STUDIES ON THE STRUCTURE AND PHOTOCHEMISTRY OF CHLOROPLAST LAMELLAE (thesis)
- Author
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John. Biggins
- Subjects
Chloroplast ,Chemistry ,Photochemistry - Published
- 1965
22. Dirty complexity: money laundering through derivatives
- Author
-
John Biggins
- Subjects
Economics and Finance, Law - Academic, Politics and Public Policy - Abstract
Although the practice of disguising the illicit origins of money dates back thousands of years, the concept of money laundering as a multidisciplinary topic with social, economic, political and regulatory implications has only gained prominence since the 1980s. This groundbreaking volume offers original, state-of-the-art research on the current money laundering debate and provides insightful predictions and recommendations for future developments in the field.
23. Bioinspired Soft Bendable Peristaltic Pump Exploiting Ballooning for High Volume Throughput
- Author
-
Leone Costi, Josephine Hughes, John Biggins, and Fumiya Iida
- Subjects
Human-Computer Interaction ,soft robotics ,Control and Optimization ,Artificial Intelligence ,Biomedical Engineering ,bioinspired robotics ,mechanical systems ,pumps ,pneumatic actuators ,Computer Science Applications - Abstract
Interest in bioinspired peristaltic pumps has grown in popularity among the scientific community in the last decade thanks to their extreme flexibility and their intrinsic compliance. In this paper, we propose a soft peristaltic pump exploiting ballooning. Our aim is to promote and propel forward the ballooned region by controlling the air pressure between the balloon and an external flexible containment tube, to achieve a peristaltic pumping motion with a simple design and using only one control signal. This paper describes the implementation of the pump and the inlet-pump-outlet system, provides an analytical model to predict the pump performance, and showcases experimental results. We also implement a computer simulation to further characterize the device. We show that it is possible to achieve high volumetric flow rates, up to 4.4 mL/s, with only a single control signal, paving the way for more flexible and easy to manufacture peristaltic pumps.
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