Open AccessThe hydE gene is essential for the formation of Wolinella succinogenes NiFe‐hydrogenase
Author(s) -
Gross Roland,
Simon Jörg
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00681-5
Subject(s) - hydrogenase , gene , carbon monoxide dehydrogenase , mutant , biology , biochemistry , protein subunit , bacteria , chemistry , enzyme , genetics , carbon monoxide , catalysis
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.