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Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
- A. Volbeda, M. Charon, C. Piras, E. Hatchikian, M. Frey, J. Fontecilla-Camps
- 16 February 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 solved at 2.85 Å resolution and suggests plausible electron and proton transfer pathways.
Microbial Ecology of Volcanic Sulphidogenesis: Isolation and Characterization of Thermodesulfobacterium commune gen. nov. and sp. nov.,
Strain YSRA-1 is described as the type strain of the new genus and species Thermodesulfobacterium commune, a new species of thermophile associated with volcanic activity in Yellowstone National Park which proliferated at temperatures above 45 °C but below 85 °C, and had an optimum growth temperature of 70 °C.
Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate
- E. Chabrière, M. Charon, A. Volbeda, L. Pieulle, E. Hatchikian, J. Fontecilla-Camps
- Chemistry, BiologyNature Structural Biology
- 1 February 1999
The PFOR–pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction, and the thiamin pyrophosphate cofactor and the three [4Fe–4S] clusters are suitably arranged to provide a plausible electron transfer pathway.
Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans.
- Y. Nicolet, A. L. De Lacey, X. Vernède, V. Fernández, E. Hatchikian, J. Fontecilla-Camps
- ChemistryJournal of the American Chemical Society
- 2 February 2001
Both stereochemical and mechanistic considerations suggest that the small organic molecule found at the Fe-only hydrogenase active site and previously modeled as 1,3-propanedithiolate may, in fact, be di-(thiomethyl)-amine.
The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center.
Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
The 2.54 Å resolution structure of Ni-Fe hydrogenase has revealed the existence of hydrophobic channels connecting the molecular surface to the active site, and a crystallographic analysis of xenon binding together with molecular dynamics simulations suggest that these channels serve as pathways for gas access to theactive site.
Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase
- E. Chabrière, X. Vernède, B. Guigliarelli, M. Charon, E. Hatchikian, J. Fontecilla-Camps
- Chemistry, BiologyScience
- 21 December 2001
The data, along with evidence from the literature, suggest that acetyl-CoA synthesis by PFOR proceeds via a condensation mechanism involving acetyl (PFOR-based) and thiyl (CoA- based) radicals.
High-resolution crystallographic analysis of Desulfovibrio fructosovorans [NiFe] hydrogenase
Structure of the [Nife] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands
Crystallographic data on the [NiFe] hydrogenase from Desulfovibrio gigas are presented that provide new information on the structure and mode of action of its dihydrogen activating metal center.…
The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy
- W. Roseboom, A. L. Lacey, V. Fernández, E. Hatchikian, S. Albracht
- ChemistryJBIC Journal of Biological Inorganic Chemistry
Electrochemical redox titrations showed that the enzyme in the Hinact state converts to the transition state (Htrans) in a reversible one-electron redox step (Em, pH 7=–75 mV), and IR spectra demonstrate that the added redox equivalent not only affects the [4Fe-4S]H subcluster, but also the di-iron centre.