Search Results - "Hatchikian, E. Claude"
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The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy
Published in Journal of biological inorganic chemistry (01-01-2006)“…In [FeFe]-hydrogenases, the H cluster (hydrogen-activating cluster) contains a di-iron centre ([2Fe]H subcluster, a…”
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The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. I. Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance
Published in Journal of biological inorganic chemistry (2006)“…The hydrogen-activating cluster (H cluster) in [FeFe]-hydrogenases consists of two moieties. The [2Fe]H subcluster is a…”
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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
Published in Nature (London) (16-02-1995)“…The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been…”
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The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway
Published in Journal of molecular biology (18-11-2005)“…In Desulfovibrio metabolism, periplasmic hydrogen oxidation is coupled to cytoplasmic sulfate reduction via transmembrane electron transfer complexes. Type II…”
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IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase
Published in Journal of biological inorganic chemistry (01-03-2002)“…The binding of carbon monoxide, a competitive inhibitor of many hydrogenases, to the active site of Desulfovibrio fructosovorans hydrogenase has been studied…”
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FTIR spectroelectrochemical study of the activation and inactivation processes of [NiFe] hydrogenases: effects of solvent isotope replacement and site-directed mutagenesis
Published in Journal of biological inorganic chemistry (01-07-2004)“…The kinetics of the activation and anaerobic inactivation processes of Desulfovibrio gigas hydrogenase have been measured in D(2)O by FTIR…”
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Spectroscopic and kinetic characterization of active site mutants of Desulfovibrio fructosovorans Ni-Fe hydrogenase
Published in Journal of biological inorganic chemistry (01-01-2003)Get full text
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Oriented immobilization of Desulfovibrio gigas hydrogenase onto carbon electrodes by covalent bonds for nonmediated oxidation of H2
Published in Journal of the American Chemical Society (23-11-2005)“…The orientation of hydrogenase bound covalently to a pyrolytic graphite edge electrode modified with a 4-aminophenyl monolayer can be modulated via…”
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The Electronic Structure of the H-Cluster in the [FeFe]-Hydrogenase from Desulfovibrio desulfuricans: A Q-band 57Fe-ENDOR and HYSCORE Study
Published in Journal of the American Chemical Society (19-09-2007)“…The active site of the 57Fe-enriched [FeFe]-hydrogenase (i.e., the “H-cluster”) from Desulfovibrio desulfuricans has been examined using advanced pulse EPR…”
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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
Published in Structure (London) (15-01-1999)“…Background: Many microorganisms have the ability to either oxidize molecular hydrogen to generate reducing power or to produce hydrogen in order to remove…”
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Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
Published in Nature structural biology (01-07-1997)“…The 2.54 A resolution structure of Ni-Fe hydrogenase has revealed the existence of hydrophobic channels connecting the molecular surface to the active site. A…”
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Disulfide Bond-Dependent Mechanism of Protection against Oxidative Stress in Pyruvate-Ferredoxin Oxidoreductase of Anaerobic Desulfovibrio Bacteria
Published in Biochemistry (Easton) (22-01-2008)“…Oxidative decarboxylation of pyruvate forming acetyl-coenzyme A is a crucial step in many metabolic pathways. In most anaerobes, this reaction is carried out…”
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Carboxy-Terminal Processing of the Large Subunit of [Fe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757
Published in Journal of Bacteriology (01-05-1999)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Structural organization of the Ni and (4Fe-4S) centers in the active form of Desulfovibrio gigas hydrogenase. Analysis of the magnetic interactions by electron paramagnetic resonance spectroscopy
Published in Biochemistry (Easton) (11-04-1995)“…The Desulfovibrio gigas hydrogenase is a typical (NiFe) hydrogenase containing a Ni center and three FeS centers, one [3Fe-4S] and two [4Fe-4S] clusters. When…”
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Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands
Published in Journal of the American Chemical Society (25-12-1996)“…Crystallographic data on the [NiFe] hydrogenase from Desulfovibrio gigas are presented that provide new information on the structure and mode of action of its…”
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FTIR Characterization of the Active Site of the Fe-hydrogenase from Desulfovibrio desulfuricans
Published in Journal of the American Chemical Society (15-11-2000)Get full text
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Crystal Structure of the Free Radical Intermediate of Pyruvate: Ferredoxin Oxidoreductase
Published in Science (American Association for the Advancement of Science) (21-12-2001)“…In anaerobic organisms, the decarboxylation of pyruvate, a crucial component of intermediary metabolism, is catalyzed by the metalloenzyme pyruvate: ferredoxin…”
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[3Fe-4S] to [4Fe-4S] Cluster Conversion in Desulfovibrio fructosovorans [NiFe] Hydrogenase by Site-Directed Mutagenesis
Published in Proceedings of the National Academy of Sciences - PNAS (29-09-1998)“…The role of the high potential [3Fe-4S]1+,0 cluster of [NiFe] hydrogenase from Desulfovibrio species located halfway between the proximal and distal low…”
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Investigation of metal ion uptake reactivities of [3Fe-4S] clusters in proteins: voltammetry of co-adsorbed ferredoxin-aminocyclitol films at graphite electrodes and spectroscopic identification of transformed clusters
Published in Journal of the American Chemical Society (01-08-1991)“…Facile transformation of Fe-S clusters in proteins, as described by (3Fe-4S) super(0) + M super(2+) (M3Fe-4S) super(2+) in which metal ion M enters the vacant…”
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Flexibility of Thiamine Diphosphate Revealed by Kinetic Crystallographic Studies of the Reaction of Pyruvate-Ferredoxin Oxidoreductase with Pyruvate
Published in Structure (London) (01-02-2006)“…Pyruvate-ferredoxin oxidoreductases (PFOR) are unique among thiamine pyrophosphate (ThDP)-containing enzymes in giving rise to a rather stable cofactor-based…”
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