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The hydE gene is essential for the formation of Wolinella succinogenes NiFe-hydrogenase.

Gross, R. and Simon, J. (2003):
The hydE gene is essential for the formation of Wolinella succinogenes NiFe-hydrogenase.
In: FEMS microbiology letters, pp. 197-202, 227, (2), ISSN 0378-1097, [Article]

Abstract

Wolinella succinogenes grows by anaerobic respiration using hydrogen gas as electron donor. The hydE gene is located on the genome downstream of the structural genes encoding the membrane-bound NiFe-hydrogenase complex (HydABC) and a putative protease (HydD) possibly involved in hydrogenase maturation. Homologs of hydE are found in the vicinity of NiFe-hydrogenase-encoding genes on the genomes of several other proteobacteria. A hydE deletion mutant of W. succinogenes does not catalyze hydrogen oxidation with various electron acceptors. The hydrogenase iron-sulfur subunit HydA is absent in mutant cells whereas the apparently processed NiFe subunit (HydB) is located exclusively in the soluble cell fraction. It is suggested that HydE is involved in the maturation and/or stability of HydA or the HydAB complex in some, but not all bacteria containing NiFe-hydrogenases.

Item Type: Article
Erschienen: 2003
Creators: Gross, R. and Simon, J.
Title: The hydE gene is essential for the formation of Wolinella succinogenes NiFe-hydrogenase.
Language: English
Abstract:

Wolinella succinogenes grows by anaerobic respiration using hydrogen gas as electron donor. The hydE gene is located on the genome downstream of the structural genes encoding the membrane-bound NiFe-hydrogenase complex (HydABC) and a putative protease (HydD) possibly involved in hydrogenase maturation. Homologs of hydE are found in the vicinity of NiFe-hydrogenase-encoding genes on the genomes of several other proteobacteria. A hydE deletion mutant of W. succinogenes does not catalyze hydrogen oxidation with various electron acceptors. The hydrogenase iron-sulfur subunit HydA is absent in mutant cells whereas the apparently processed NiFe subunit (HydB) is located exclusively in the soluble cell fraction. It is suggested that HydE is involved in the maturation and/or stability of HydA or the HydAB complex in some, but not all bacteria containing NiFe-hydrogenases.

Journal or Publication Title: FEMS microbiology letters
Volume: 227
Number: 2
Divisions: 10 Department of Biology > Microbial Energy Conversion and Biotechnology
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10 Department of Biology
Date Deposited: 07 Dec 2010 15:17
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