H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha
Autor: | Stefanie Ganskow, Bärbel Friedrich, Tobias Goris, Torsten Schubert, Marcus Ludwig, Ingmar Bürstel, Oliver Lenz, Alexander Schwarze |
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Rok vydání: | 2010 |
Předmět: |
Hydrogenase
biology Chemistry Stereochemistry Active site biology.organism_classification Photochemistry Atomic and Molecular Physics and Optics Reversible reaction Cofactor Catalysis Metal Oxygen Ralstonia Biocatalysis visual_art Catalytic Domain biology.protein visual_art.visual_art_medium Cupriavidus necator Physical and Theoretical Chemistry Oxidation-Reduction Hydrogen |
Zdroj: | Chemphyschem : a European journal of chemical physics and physical chemistry. 11(6) |
ISSN: | 1439-7641 |
Popis: | [NiFe]-hydrogenases catalyze the oxidation of H(2) to protons and electrons. This reversible reaction is based on a complex interplay of metal cofactors including the Ni-Fe active site and several [Fe-S] clusters. H(2) catalysis of most [NiFe]-hydrogenases is sensitive to dioxygen. However, some bacteria contain hydrogenases that activate H(2) even in the presence of O(2). There is now compelling evidence that O(2) affects hydrogenase on three levels: 1) H(2) catalysis, 2) hydrogenase maturation, and 3) H(2)-mediated signal transduction. Herein, we summarize the genetic, biochemical, electrochemical, and spectroscopic properties related to the O(2) tolerance of hydrogenases resident in the facultative chemolithoautotroph Ralstonia eutropha H16. A focus is given to the membrane-bound [NiFe]-hydogenase, which currently represents the best-characterized member of O(2)-tolerant hydrogenases. |
Databáze: | OpenAIRE |
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