| A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress. | |
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MedLine Citation:
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PMID: 14594815 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sulfate-reducing bacteria, like Desulfovibrio vulgaris Hildenborough, have developed a set of reactions allowing them to survive in oxic environments and even to reduce molecular oxygen to water. D. vulgaris contains a cytoplasmic superoxide reductase (SOR) and a periplasmic superoxide dismutase (SOD) involved in the elimination of superoxide anions. To assign the function of SOD, the periplasmic [Fe] hydrogenase activity was followed in both wild-type and sod deletant strains. This activity was lower in the strain lacking the SOD than in the wild-type when the cells were exposed to oxygen for a short time. The periplasmic SOD is thus involved in the protection of sensitive iron-sulfur-containing enzyme against superoxide-induced damages. Surprisingly, production of the periplasmic [Fe] hydrogenase was higher in the cells exposed to oxygen than in those kept in anaerobic conditions. A similar increase in the amount of [Fe] hydrogenase was observed when an increase in the redox potential was induced by addition of chromate. Viability of the strain lacking the gene encoding [Fe] hydrogenase after exposure to oxygen for 1 h was lower than that of the wild-type. These data reveal for the first time that production of the periplasmic [Fe] hydrogenase is up-regulated in response to an oxidative stress. A new function of the periplasmic [Fe] hydrogenase in the protective mechanisms of D. vulgaris Hildenborough toward an oxidative stress is proposed. |
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Authors:
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Marjorie Fournier; Zorah Dermoun; Marie-Claire Durand; Alain Dolla |
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Publication Detail:
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Type: Journal Article Date: 2003-10-31 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 279 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2004 Jan |
Date Detail:
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Created Date: 2004-01-12 Completed Date: 2004-02-12 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 1787-93 Citation Subset: IM |
Affiliation:
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Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS 31, Chemin Joseph Aiguier, 13402 Marseille cedex 20, France. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Desulfovibrio vulgaris
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enzymology* Hydrogenase / physiology* Iron-Sulfur Proteins / physiology* Oxidative Stress* Superoxide Dismutase / physiology |
| Chemical | |
Reg. No./Substance:
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0/Iron-Sulfur Proteins; EC 1.12.-/iron hydrogenase; EC 1.12.7.2/Hydrogenase; EC 1.15.1.1/Superoxide Dismutase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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