Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Claude E. Hatchikian"'
Autor:
Mirjam Czjzek, Latifa Elantak, Françoise Guerlesquin, Alain Dolla, Claude E. Hatchikian, Xavier Morelli, Olivier Bornet
Publikováno v:
FEBS Letters. 548:1-4
Cytochrome c3 (Mr 13 000) is a low redox potential cytochrome specific of the anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in Desulfovibrio vulgar
Autor:
Claude E. Hatchikian, Jürgen Hüttermann, Richard Cammack, Reinhard Kappl, Arnd Müller, Irene Tscherny
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 7:177-194
Hydrons and electrons are substrates for the enzyme hydrogenase, but cannot be observed in X-ray crystal structures. High-resolution 1H electron nuclear double resonance (ENDOR) spectroscopy offers a means to detect the distribution of protons and un
Autor:
Claude E. Hatchikian, Mirjam Czjzek, Juan C. Fontecilla-Camps, José J. G. Moura, Françoise Guerlesquin, Nuno Palma, Olivier Bornet, Xavier Morelli
Publikováno v:
Journal of Biological Chemistry. 275:23204-23210
Fe-hydrogenase is a 54-kDa iron-sulfur enzyme essential for hydrogen cycling in sulfate-reducing bacteria. The x-ray structure of Desulfovibrio desulfuricans Fe-hydrogenase has recently been solved, but structural information on the recognition of it
Publikováno v:
Journal of Molecular Biology. 290:881-902
Unique among sulphate-reducing bacteria, Desulfovibrio africanus has two periplasmic tetraheme cytochromes c 3 , one with an acidic isoelectric point which exhibits an unusually low reactivity towards hydrogenase, and another with a basic isoelectric
Autor:
Pierre Legrand, Claudine Piras, Yvain Nicolet, Claude E. Hatchikian, Juan C. Fontecilla-Camps
Publikováno v:
Structure. 7:13-23
Background: Many microorganisms have the ability to either oxidize molecular hydrogen to generate reducing power or to produce hydrogen in order to remove low-potential electrons. These reactions are catalyzed by two unrelated enzymes: the Ni–Fe hy
Autor:
Claude E. Hatchikian, Juan-Carlos Fontecilla-Camps, Elsa D. Garcin, Anne Volbeda, Yaël Montet, Michel Frey
Publikováno v:
Pure and Applied Chemistry. 70:25-31
bar of H2). However, hydrogen oxidation is not energetically favourable because of the very low acidity of the H-H bond (pKa = 35). This can be dramatically changed through binding of molecular hydrogen to a metal center since the pKa can be lowered
Autor:
X. Vernede, Elsa D. Garcin, Yaël Montet, Michel Frey, Anne Volbeda, Claudine Piras, Juan-Carlos Fontecilla-Camps, Claude E. Hatchikian
Publikováno v:
Biochimie. 79:661-666
Hydrogenases are proteins which metabolize the most simple of chemical compounds, molecular hydrogen, according to the reaction H2 ↔ 2H+ + 2e−. These enzymes are found in many microorganisms of great biotechnological interest such as methanogenic
Autor:
Victor M. Fernandez, Christine Cavazza, Antonio L. De Lacey, Claude E. Hatchikian, Marc Rousset
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 8(1-2)
Site-directed mutagenesis of amino acid residues proximate to the active site of the Ni-Fe hydrogenase of Desulfovibrio fructosovorans has been done. The different mutants have been analyzed by FTIR spectroscopy and compared with wild type enzyme. Th
Autor:
Hua-Jun Fan, Antonio L. De Lacey, Shuhua Li, Victor M. Fernandez, Christian Stadler, Michael B. Hall, Claude E. Hatchikian
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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25 páginas, 9 figuras y 2 tablas
The binding of carbon monoxide a competitive inhibitor of many hydrogenases, to the active site of Desulfovibrio fructosovorans hydrogenase has been studied by infrared spectroscopy in a spectroelectrochemical c
The binding of carbon monoxide a competitive inhibitor of many hydrogenases, to the active site of Desulfovibrio fructosovorans hydrogenase has been studied by infrared spectroscopy in a spectroelectrochemical c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9846b3d4abd353e046a71f51f513a8a6
http://hdl.handle.net/10261/99241
http://hdl.handle.net/10261/99241
Autor:
Anne Volbeda, Claude E. Hatchikian, Michel Frey, Elsa D. Garcin, Yaël Montet, Juan-Carlos Fontecilla-Camps
Publikováno v:
ResearcherID