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This paper reports the first example of C-H arylation of benzene under mild conditions, using H2 as an electron source {turnover numbers (TONs)=0.7-2.0 for 24 h}. The reaction depends on a Rh-based electron storage catalyst, and proceeds at room temperature and in aqueous solution. Furthermore, the H2 is inactive during the radical transfer step, greatly reducing unwanted side reactions.

Four requirements for the reductive C(sp3)–C(sp3) homo-coupling of benzyl/allyl halides in aqueous solution by using H2 as an electron source are described.

The DNA‐binding protein from starved cells (Dps) is found in a wide range of microorganisms, and it has been well characterized. However, little is known about Dps proteins from nonheterocystous filamentous cyanobacteria. In this study, a Dps protein from the thermophilic nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 demonstrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein, which presumably contributed to its exceedingly high thermostability., A DNA‐binding protein from starved cells (Dps) protein from nonheterocystous filamentous cyanobacterium Thermoleptolyngbya sp. O‐77 (TlDps1) was purified and characterized. PAGE and CD analyses of TlDps1 illustrated that it had higher thermostability than previously reported Dps proteins. X‐ray crystallographic analysis revealed that TlDps1 possessed His‐type ferroxidase centers within the cavity and unique metal‐binding sites located on the surface of the protein.

We present a novel fuel cell heterogeneous catalyst based on rhodium, nickel and sulfur with power densities 5–28% that of platinum. The NiRhS heterogeneous catalyst was developed via a homogeneous model complex of the [NiFe]hydrogenases (H2ases) and can act as both the cathode and anode of a fuel cell.

This paper reports the first example of a reductive C(sp

C-phycocyanin (CPC), a blue pigment protein, is an indispensable component of giant phycobilisomes, which are light-harvesting antenna complexes in cyanobacteria that transfer energy efficiently to photosystems I and II. X-ray crystallographic and electron microscopy (EM) analyses have revealed the structure of CPC to be a closed toroidal hexamer by assembling two trimers. In this study, the structural characterization of non-conventional octameric CPC is reported for the first time. Analyses of the crystal and cryogenic EM structures of the native CPC from filamentous thermophilic cyanobacterium Thermoleptolyngbya sp. O–77 unexpectedly illustrated the coexistence of conventional hexamer and novel octamer. In addition, an unusual dimeric state, observed via analytical ultracentrifugation, was postulated to be a key intermediate structure in the assemble of the previously unobserved octamer. These observations provide new insights into the assembly processes of CPCs and the mechanism of energy transfer in the light-harvesting complexes., Takuo Minato and colleagues determine the crystal and cryo-EM structures of the native C-phycocyanin (CPC) from the thermophilic cyanobacterium, Thermoleptolyngbya sp. O77, which was found to adopt both a conventional hexameric structure and a novel octameric assembly. These findings provide new insights into the assembly of CPCs and their mechanism of energy transfer.

This paper reports a possible mechanism of acetic acid formation from CO2, CH3I and H2 in aqueous media and the central role played by a water-soluble Rh-based electron storage catalyst. In addition to water-solubility, we also report the crystal structures of two presumed intermediates. These findings together reveal (1) the advantage of water, not only as a green solvent, but also as a reactive Lewis base to extract H+ from H2, (2) the role of the metal (Rh) centre as a point for storing electrons from H2 and (3) the importance of an electron-withdrawing ligand (quaterpyridine, qpy) that supports electron storage.

This paper reports the first example of C-H arylation of benzene under mild conditions, using H

This paper reports a possible mechanism of acetic acid formation from CO2, CH3I and H2 in aqueous media and the central role played by a water-soluble Rh-based electron storage catalyst. In addition to water-solubility, we also report the crystal structures of two presumed intermediates. These findings together reveal (1) the advantage of water, not only as a green solvent, but also as a reactive Lewis base to extract H+ from H2, (2) the role of the metal (Rh) centre as a point for storing electrons from H2 and (3) the importance of an electron-withdrawing ligand (quaterpyridine, qpy) that supports electron storage.

Three isomers of the same NiFe complex can mimic the catalytic properties of [NiFe], [FeFe], and [Fe] hydrogenase enzymes., The study of hydrogenase enzymes (H2ases) is necessary because of their importance to a future hydrogen energy economy. These enzymes come in three distinct classes: [NiFe] H2ases, which have a propensity toward H2 oxidation; [FeFe] H2ases, which have a propensity toward H2 evolution; and [Fe] H2ases, which catalyze H− transfer. Modeling these enzymes has so far treated them as different species, which is understandable given the different cores and ligand sets of the natural molecules. Here, we demonstrate, using x-ray analysis and nuclear magnetic resonance, infrared, Mössbauer spectroscopies, and electrochemical measurement, that the catalytic properties of all three enzymes can be mimicked with only three isomers of the same NiFe complex.

The development of hydrogen fuel cells is greatly hindered by the unwanted generation of H2 O2 at the cathode. A non-Pt cathode catalyst is now shown to be capable of simultaneously reducing both O2 and H2 O2 , thus rendering H2 O2 a useful part of the feed stream. The applicability of this unique catalyst is demonstrated by employing it in a fuel cell running on H2 /CO and O2 /H2 O2 .

Oxidative damage of DNA by reactive oxygen species (ROS) is responsible for aging and cancer. Although many studies of DNA damage by ROS have been conducted, there have been no reports of the oxidation of RNA components, such as guanosine monophosphate, by metal-based species in water. Here, we report the first case of oxidation of guanosine monophosphate to 8-oxoguanosine monophosphate by a metal-based oxygen bound species, derived from O2 and in water.

Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe–4S] cluster proximal to the Ni–Fe active site. The presence of relocatable water molecules and a flexible aspartate enables the [4Fe–4S] to display redox-dependent conformational changes. These structural features are proposed to be the key aspects that protect the active site from O2 attack.

We report the mechanistic investigation of catalytic H2 evolution from formic acid in water using a formate-bridged dinuclear Ru complex as a formate hydrogen lyase model. The mechanistic study is based on isotope-labeling experiments involving hydrogen isotope exchange reaction., Graphical Abstract

We present a mechanistic investigation for the activation of H2 and O2, induced by a simple ligand effect within [NiFe] models for O2-tolerant [NiFe]hydrogenase. Kinetic study reveals Michaelis–Menten type saturation behaviors for both H2 and O2 activation, which is the same behavior as that found in O2-tolerant [NiFe]hydrogenase. Such saturation behavior is caused by H2 complexation followed by heterolytic cleavage of H2 by an outer-sphere base, resulting in the formation of a hydride species showing hydridic character.

We report an Ir complex as an anode catalyst capable of switching between a hydrogenase-type fuel-cell mode and a photosystem II-type solar-cell mode. This catalyst is connected to carbon-black-supported platinum as a cathode catalyst, which reduces dioxygen in a manner analogous to cytochrome c oxidase. Together, they make a system capable of switching between the two modes.

How a hydrogenase protects its active site Hydrogen-metabolizing organisms use an [NiFe]-hydrogenase to catalyze hydrogen oxidation. One type of [NiFe]-hydrogenase, the NAD + -reducing soluble [NiFe]-hydrogenase (SH), couples reduction of NAD + to the oxidation of hydrogen. Shomura et al. solved the structure of SH from an H 2 -oxidizing bacterium in both the air-oxidized and the active reduced state. In the reduced state, the NiFe catalytic center in SH has the same ligand coordination as in other [NiFe]-hydrogenases. However, the air-oxidized active site has an unusual coordination geometry that would prevent O 2 from accessing the site and so may protect against irreversible oxidation. Science , this issue p. 928

Pyruvate ferredoxin oxidoreductase from Citrobacter sp. S-77 (PFORS77) was purified in order to develop a method for acetyl-CoA production. Although the purified PFORS77 showed high O2-sensitivity, the activity could be remarkably stabilized in anaerobic conditions. PFORS77 was effectively immobilized on ceramic hydroxyapatite (PFORS77-HA) with an efficiency of more than 96%, however, after encapsulation of PFORS77-HA in alginate, the rate of catalytic acetyl-CoA production was highly reduced to 36% when compared to that of the free enzyme. However, the operational stability of the PFORS77-HA in alginate hydrogels was remarkable, retaining over 68% initial activity even after ten repeated cycles. The results suggested that the PFORS77-HA hydrogels have a high potential for biotechnological application.

Cyanobacteria are widely distributed in marine, aquatic, and terrestrial ecosystems, and play an important role in the global nitrogen cycle. In the present study, we examined the genome sequence of the thermophilic non-heterocystous N2-fixing cyanobacterium, Thermoleptolyngbya sp. O-77 (formerly known as Leptolyngbya sp. O-77) and characterized its nitrogenase activity. The genome of this cyanobacterial strain O-77 consists of a single chromosome containing a nitrogen fixation gene cluster. A phylogenetic analysis indicated that the NifH amino acid sequence from strain O-77 was clustered with those from a group of mesophilic species: the highest identity was found in Leptolyngbya sp. KIOST-1 (97.9% sequence identity). The nitrogenase activity of O-77 cells was dependent on illumination, whereas a high intensity of light of 40 μmol m-2 s-1 suppressed the effects of illumination.

We report the reactivity of a new MnI(cyclam) complex (cyclam: 1,4,8,11-tetraazacyclotetradecane) toward O2 and H2O as a model for the photoinhibited species of oxygen-evolving complex (OEC). The reactivity varies according to the number of CO ligands. A MnI dicarbonyl complex, [MnI(cyclam)(CO)2]+ reacts with O2, but not with H2O, to form a bis(μ-oxo)Mn2III,IV complex, though a MnI tricarbonyl complex, [MnI(cyclam)(CO)3]+ does not react with either O2 or H2O. Newly synthesized MnI(cyclam) dicarbonyl complex was characterized by ESI mass spectrometry, UV–vis absorption spectroscopy, IR spectroscopy, and X-ray analysis.

The purification procedure of Hyd-2-type [NiFe]-hydrogenase fromCitrobactersp. S-77 was improved by applying treatment with trypsin before chromatography. Purified protein samples both with and without trypsin treatment were successfully crystallized using the sitting-drop vapour-diffusion method with polyethylene glycol as a precipitant. Both crystals belonged to space groupP21, with unit-cell parametersa= 63.90,b= 118.89,c= 96.70 Å, β = 100.61° for the protein subjected to trypsin treatment anda= 65.38,b= 121.45,c= 98.63 Å, β = 102.29° for the sample not treated with trypsin. The crystal obtained from the trypsin-treated protein diffracted to 1.60 Å resolution, which is considerably better than the 2.00 Å resolution obtained without trypsin treatment. The [NiFe]-hydrogenase fromCitrobactersp. S-77 retained catalytic activity with some amount of O2, indicating that it has clear O2tolerance.

We report the first example of the characterization of a Ru-based peroxide intermediate of O2-promoted activation of a C–H bond of the pentamethylcyclopentadienyl (Cp*) ligand. The peroxide complex activates the C–H bond to form a tetramethylfulvene complex. We propose a proton-coupled electron-transfer (PCET) mechanism of the C–H bond activation based on the structures and properties of the peroxide and tetramethylfulvene complexes.

Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe-4S] cluster proximal to the Ni-Fe active site. The presence of relocatable water molecules and a flexible aspartate enables the [4Fe-4S] to display redox-dependent conformational changes. These structural features are proposed to be the key aspects that protect the active site from O2 attack.

The development of hydrogen fuel cells is greatly hindered by the unwanted generation of H

Oxidative damage of DNA by reactive oxygen species (ROS) is responsible for aging and cancer. Although many studies of DNA damage by ROS have been conducted, there have been no reports of the oxidation of RNA components, such as guanosine monophosphate, by metal-based species in water. Here, we report the first case of oxidation of guanosine monophosphate to 8-oxoguanosine monophosphate by a metal-based oxygen bound species, derived from O

Protein CoAlation (S-thiolation by coenzyme A) has recently emerged as an alternative redox-regulated post-translational modification by which protein thiols are covalently modified with coenzyme A (CoA). However, little is known about the role and mechanism of this post-translational modification. In the present study, we investigated CoAlation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from a facultative anaerobic Gram-negative bacterium Citrobacter sp. S-77 (Cb GAPDH). GAPDH is a key glycolytic enzyme whose activity relies on the thiol-based redox-regulated post-translational modifications of active-site cysteine. LC-MS/MS analysis revealed that CoAlation of Cb GAPDH occurred in vivo under sodium hypochlorite (NaOCl) stress. The purified Cb GAPDH was highly sensitive to overoxidation by H2O2 and NaOCl, which resulted in irreversible enzyme inactivation. By contrast, treatment with coenzyme A disulphide (CoASSCoA) or H2O2/NaOCl in the presence of CoA led to CoAlation and inactivation of the enzyme; activity could be recovered after incubation with dithiothreitol, glutathione and CoA. CoAlation of the enzyme in vitro was confirmed by mass spectrometry. The presence of a substrate, glyceraldehyde-3-phosphate, fully protected Cb GAPDH from inactivation by CoAlation, suggesting that the inactivation is due to the formation of mixed disulphides between CoA and the active-site cysteine Cys149. A molecular docking study also supported the formation of mixed disulphide without steric constraints. These observations suggest that CoAlation is an alternative mechanism to protect the redox-sensitive thiol (Cys149) of Cb GAPDH against irreversible oxidation, thereby regulating enzyme activity under oxidative stress.

The class of [NiFe]-hydrogenases comprises oxygen-sensitive periplasmic (PH) and oxygen-tolerant membrane-bound (MBH) enzymes. For three PHs and four MBHs from six bacterial species, structural features of the nickel–iron active site of hydrogen turnover and of the iron–sulfur clusters functioning in electron transfer were determined using X-ray absorption spectroscopy (XAS). Fe-XAS indicated surplus oxidized iron and a lower number of ~ 2.7 Å Fe–Fe distances plus additional shorter and longer distances in the oxidized MBHs compared to the oxidized PHs. This supported a double-oxidized and modified proximal FeS cluster in all MBHs with an apparent trimer-plus-monomer arrangement of its four iron atoms, in agreement with crystal data showing a [4Fe3S] cluster instead of a [4Fe4S] cubane as in the PHs. Ni-XAS indicated coordination of the nickel by the thiol group sulfurs of four conserved cysteines and at least one iron–oxygen bond in both MBH and PH proteins. Structural differences of the oxidized inactive [NiFe] cofactor of MBHs in the Ni-B state compared to PHs in the Ni–A state included a ~ 0.05 Å longer Ni-O bond, a two times larger spread of the Ni–S bond lengths, and a ~ 0.1 Å shorter Ni–Fe distance. The modified proximal [4Fe3S] cluster, weaker binding of the Ni–Fe bridging oxygen species, and an altered localization of reduced oxygen species at the active site may each contribute to O2 tolerance., M.H. thanks the Deutsche Forschungsgemeinschaft (DFG) for a Heisenberg Fellowship and the DFG (grants Ha3265/3-1 and Ha3265/6-1) and the Bundesministerium für Bildung und Wissenschaft (grant 05K14KE1 within the Röntgen-Angström Cluster) for the financial support. A.L.D.L thanks MINECO (project CTQ2012-32448) for the financial support. F.A.A. is a Royal Society Wolfson Research Merit Award holder.

Reported herein is an electrode for dihydrogen (H2) oxidation, and it is based on [NiFe]Hydrogenase from Citrobacter sp. S-77 ([NiFe]S77). It has a 637 times higher mass activity than Pt (calculated based on 1 mg of [NiFe]S77 or Pt) at 50 mV in a hydrogen half-cell. The [NiFe]S77 electrode is also stable in air and, unlike Pt, can be recovered 100 % after poisoning by carbon monoxide. Following characterization of the [NiFe]S77 electrode, a fuel cell comprising a [NiFe]S77 anode and Pt cathode was constructed and shown to have a a higher power density than that achievable by Pt.

Many types of superoxide dismutases have been purified and characterized from various bacteria, however, a psychrophilic Mn-superoxide dismutase (MnSOD) has not yet been reported. Here, we describe the purification and the biochemical characterization of the psychrophilic MnSOD from Exiguobacterium sp. strain OS-77 (EgMnSOD). According to 16S rRNA sequence analysis, a newly isolated bacterium strain OS-77 belongs to the genus Exiguobacterium. The optimum growth temperature of the strain OS-77 is 20 °C. The EgMnSOD is a homodimer of 23.5 kDa polypeptides determined by SDS-PAGE and gel filtration analysis. UV-Vis spectrum and ICP-MS analysis clearly indicated that the homogeneously purified enzyme contains only a Mn ion as a metal cofactor. The optimal reaction pH and temperature of the enzyme were pH 9.0 and 5 °C, respectively. Notably, the purified EgMnSOD was thermostable up to 45 °C and retained 50% activity after 21.2 min at 60 °C. The differential scanning calorimetry also indicated that the EgMnSOD is thermostable, exhibiting two protein denaturation peaks at 65 and 84 °C. The statistical analysis of amino acid sequence and composition of the EgMnSOD suggests that the enzyme retains psychrophilic characteristics.

The purpose of this study was designed to analyze the effects mobilization and active stretching on the difference of weight-bearing distribution, low back pain, and flexibility in pronated-foot subjects. The subjects of this study were 16 chronic low back pain patients. They were randomly divided into the control and experimental group. The experimental group had used the model of ankle mobilization and calf muscle active stretching three times per week, for 4 weeks. The control group did same method without an ankle mobilization. The range of flexion and extension motion of the lumbar vertebrae and low back pain degree and difference of weight-bearing were measured before and after the experiment. The model of ankle mobilization and calf muscle stretching of pronated-foot significantly improved the range of flexion and extension motion of the vertebrae. And the visual analogue scale and distribution of weight-bearing were decreased in both of two groups. In other word, the exercise of this study showed that the model of ankle mobilization and calf muscle stretching of pronated-foot had positive effects on improving the range of flexion and extension motion of the vertebrae. The calf muscle stretching was easy and it is effective in therapy that patients by themselves and helped to recover the balance of the vertebrae to combine ankle mobilization and muscle stretching.

[NiFeSe]hydrogenases are promising biocatalysts in H2-based technology due to their high catalytic activity and O2-stability. Here, we report purification and characterization of a new membrane-associated [NiFeSe]hydrogenase from Desulfovibrio vulgaris Miyazaki F ([NiFeSe]DvMF). The [NiFeSe]DvMF was composed of two subunits, corresponding to a large subunit of 58.3 kDa and a small subunit of 29.3 kDa determined by SDS-PAGE. Unlike conventional [NiFeSe]hydrogenases having catalytic bias toward H2-production, the [NiFeSe]DvMF showed 11-fold higher specific activity of H2-oxidation (2444 U/mg) than that of H2-production (217 U/mg). At the optimal reaction temperature of the enzyme (65°C), the specific activity of H2-oxidation could reach up to 21,553 U/mg. Amperometric assays of the [NiFeSe]DvMF clearly indicated that the enzyme had a remarkable O2-stability. According to the amino acid sequence alignment, the conserved cysteine residue at position 281 in medial cluster of other [NiFeSe]hydrogenases was specifically replaced by a serine residue (Ser281) in the [NiFeSe]DvMF. These results indicate that the [NiFeSe]DvMF can play as a new H2-oxidizing and O2-stable biocatalyst, along with providing helpful insights into the structure-function relationship of [NiFeSe]hydrogenases.

Hydrogenases are of great interest due to their potential use in H(2)-based technology. However, most hydrogenases are highly sensitive to O(2), which have been the major bottleneck in hydrogenase studies. Here we report an O(2)-stable membrane-bound [NiFe]hydrogenase (MBH) purified from a newly isolated strain, S-77. According to the 16S rRNA gene sequence and phylogenetic analysis of the strain S-77, it belongs to the genus of Citrobacter. In vitro experiments using the cytoplasmic membrane of strain S-77 suggested that a cytochrome b acts as the physiological electron acceptor of the MBH. The purified MBH was composed of a dimer of heterodimers, consisting of two distinct subunits with the molecular weights of 58.5 and 38.5 kDa. The enzyme showed a specific activity for H(2)-oxidation of 661 U/mg, which is 35-fold greater than that for H(2)-production of 18.7 U/mg. Notably, the MBH showed a remarkable O(2)-stability, maintaining almost 95% of its original activity even after incubation for 30 h in air at 4°C. These results suggest that the O(2)-stable MBH may play an important role in the H(2)-metabolic pathway under the aerobic conditions of Citrobacter sp. S-77. This is the first report of the purification and biochemical characterization of an O(2)-stable MBH from the genus of Citrobacter.

The membrane-bound [NiFe]-hydrogenase from Hydrogenovibrio marinus (HmMBH) was purified homogeneously under anaerobic conditions. Its molecular weight was estimated as 110 kDa, consisting of a heterodimeric structure of 66 kDa and 37 kDa subunits. The purified enzyme exhibited high activity in a wide temperature range: 185 U/mg at 30 °C and 615 U/mg at 85 °C (the optimum temperature). The Km and kcat/Km values for H2 were, respectively, 12 μM and 8.58 × 107 M−1 s−1. The optimum reaction pH was 7.8, but its stability was particularly high at pH 4.0–7.0. Results show that HmMBH was remarkably thermostable and oxygen-resistant: its half-life was 75 h at 80 °C under H2, and more than 72 h at 4 °C under air. The air-oxidized HmMBH for 72 h showed only weak EPR signals of Ni–B, suggesting a structural feature in which the active center is not easily oxidized.

We report the synthesis of mononuclear nonheme manganese(V)–oxo complexes in aqueous acetonitrile solution from the reaction of manganese(III) complexes using hydrogen peroxide as an oxidant for th...

Acetaldehyde-alcohol dehydrogenase (ADHE) is a bifunctional enzyme consisting of two domains of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase (ADH). The enzyme is known to be important in the cellular alcohol metabolism. However, the role of coenzyme A-acylating ADHE responsible for ethanol production from acetyl-CoA remains uncertain. Here, we present the purification and biochemical characterization of an ADHE from Citrobacter sp. S-77 (ADHE(S77)). Interestingly, the ADHE(S77) was unable to be solubilized from membrane with detergents either 1% Triton X-100 or 1% Sulfobetaine 3-12. However, the enzyme was easily dissociated from membrane by high-salt buffers containing either 1.0 M NaCl or (NH(4))(2)SO(4) without detergents. The molecular weight of a native protein was estimated as approximately 400 kDa, consisting of four identical subunits of 96.3 kDa. Based on the specific activity and kinetic analysis, the ADHES77 tended to have catalytic reaction towards acetaldehyde elimination rather than acetaldehyde formation. Our experimental observation suggests that the ADHES77 may play a pivotal role in modulating intracellular acetaldehyde concentration.

This study is concerned with structural integrity evaluations for the interference-fit flywheels in reactor coolant pumps (RCPs) of nuclear power plants. Stresses in the flywheel due to the shrinkage loads and centrifugal loads at the RCP normal operation speed, design overspeed and joint-release speed are obtained using the finite element method (FEM), where release of the deformation-controlled stresses as a result of structural interactions during rotation is considered. Fracture mechanics evaluations for a series of cracks assumed to exist in the flywheel are conducted, considering ductile (fatigue) and non-ductile fracture, and stress intensity factors are obtained for the cracks using the finite element alternating method (FEAM). From analysis results, it is found that fatigue crack growth rates calculated are negligible for smaller cracks. Meanwhile, the material resistance to non-ductile fracture in terms of the critical stress intensity factor(K IC) and the nil-ductility transition reference temperature RTinNDT are governing factors for larger cracks.

The penetration depth of cobalt silicide layer in shallow junction is assessed using the current–voltage curve both in reverse and forward bias regions. The reverse leakage current characteristics said that silicide has affected both of the areal and peripheral intensive n+/p diodes because the leakage current is increased about one order of magnitude by silicidation. In case of p+/n junction, there is no increase of reverse leakage current. In case of forward region, however, only the forward current of peripheral intensive diode was increased by silicidation. From the different junction current behavior in forward and reverse bias region, it can be said that the penetrated depth of silicide layer is almost near to the space charge region but not into it for area diode. However, in case of peripheral intensive diode, silicide has penetrated into the space charge region. The Schottky contact area formed by silicide penetration is extracted as 3.02 µm2. The extracted Schottky barrier for n+/p parameter diode is 0.63 eV which is quite similar to the theoretical value of 0.64 eV.

We report the decomposition of formic acid to hydrogen and carbon dioxide, catalysed by a NiRu complex originally developed as a [NiFe]hydrogenase model. This is the first example of H2 evolution, catalysed by a [NiFe]hydrogenase model, which does not require additional energy.

Herein, we report the first crystal structure of a monomeric p-semiquinonato d-block complex and its reactivity toward dioxygen, closely associated with a biological system of an oxygen evolving centre of photosystem II.

Membrane-bound formate dehydrogenase (FDH) was purified to homogeneity from a facultative anaerobic bacterium Citrobacter sp. S-77. The FDH from Citrobacter sp. S-77 (FDHS77) was a monomer with molecular mass of approximately 150 kDa. On SDS-PAGE, the purified FDHS77 showed as three different protein bands with molecular mass of approximately 95, 87, and 32 kDa, respectively. Based on the N-terminal amino acid sequence analysis, the sequence alignments observed for the 87 kDa protein band were identical to that of the large subunit of 95 kDa, indicating that the purified FDHS77 consisted of two subunits; a 95 kDa large subunit and a 32 kDa small subunit. The purified FDHS77 in this purification did not contain a heme b subunit, but the FDHS77 showed significant activity for formate oxidation, determined by the Vmax of 30.4 U/mg using benzyl viologen as an electron acceptor. The EPR and ICP-MS spectra indicate that the FDHS77 is a molybdenum-containing enzyme, displaying a remarkable O2-stability along with thermostability and pH resistance. This is the first report of the purification and characterization of a FDH from Citrobacter species.

Rubredoxin (Rd) from the moderately thermophilic green sulfur bacterium Chlorobium tepidum was found to function as an electron acceptor for pyruvate ferredoxin oxidoreductase (PFOR). This enzyme, which catalyzes the conversion of pyruvate to acetyl-CoA and CO(2), exhibited an absolute dependence upon the presence of Rd. However, Rd was incapable of participating in the pyruvate synthase or CO(2) fixation reaction of C. tepidum PFOR, for which two different reduced ferredoxins are employed as electron donors. These results suggest a specific functional role for Rd in pyruvate oxidation and provide the initial indication that the two important physiological reactions catalyzed by PFOR/pyruvate synthase are dependent on different electron carriers in the cell. The UV-visible spectrum of oxidized Rd, with a monomer molecular weight of 6500, gave a molar absorption coefficient at 492 nm of 6.89 mM(-1) cm(-1) with an A(492)/A(280) ratio of 0.343 and contained one iron atom/molecule. Further spectroscopic studies indicated that the CD spectrum of oxidized C. tepidum Rd exhibited a unique absorption maximum at 385 nm and a shoulder at 420 nm. The EPR spectrum of oxidized Rd also exhibited unusual anisotropic resonances at g = 9.675 and g = 4.322, which is composed of a narrow central feature with broader shoulders to high and low field. The midpoint reduction potential of C. tepidum Rd was determined to be -87 mV, which is the most electronegative value reported for Rd from any source.