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

Gross, R. ; Simon, J. (2003)
The hydE gene is essential for the formation of Wolinella succinogenes NiFe-hydrogenase.
In: FEMS microbiology letters, 227 (2)
Artikel, Bibliographie

Kurzbeschreibung (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.

Typ des Eintrags: Artikel
Erschienen: 2003
Autor(en): Gross, R. ; Simon, J.
Art des Eintrags: Bibliographie
Titel: The hydE gene is essential for the formation of Wolinella succinogenes NiFe-hydrogenase.
Sprache: Englisch
Publikationsjahr: 2003
Titel der Zeitschrift, Zeitung oder Schriftenreihe: FEMS microbiology letters
Jahrgang/Volume einer Zeitschrift: 227
(Heft-)Nummer: 2
Kurzbeschreibung (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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology
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10 Fachbereich Biologie
Hinterlegungsdatum: 07 Dez 2010 15:17
Letzte Änderung: 05 Mär 2013 09:42
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