Document Detail

A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress.
MedLine Citation:
PMID:  14594815     Owner:  NLM     Status:  MEDLINE    
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.
Marjorie Fournier; Zorah Dermoun; Marie-Claire Durand; Alain Dolla
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Publication Detail:
Type:  Journal Article     Date:  2003-10-31
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  279     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-01-12     Completed Date:  2004-02-12     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1787-93     Citation Subset:  IM    
Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS 31, Chemin Joseph Aiguier, 13402 Marseille cedex 20, France.
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MeSH Terms
Desulfovibrio vulgaris / enzymology*
Hydrogenase / physiology*
Iron-Sulfur Proteins / physiology*
Oxidative Stress*
Superoxide Dismutase / physiology
Reg. No./Substance:
0/Iron-Sulfur Proteins; EC 1.12.-/iron hydrogenase; EC; EC Dismutase

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