The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
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منابع مشابه
A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris (Hildenborough).
Rubrerythrin is a nonheme iron protein of unknown function isolated from Desulfovibrio vulgaris (Hildenborough). We have sequenced a 3.3-kbp Sal1 fragment of D. vulgaris chromosomal DNA containing the rubrerythrin gene, rbr, identified additional open reading frames (ORFs) adjacent to rbr, and shown that these ORFs are part of a transcriptional unit containing rbr. One ORF, designated fur, lies...
متن کاملCarbon monoxide cycling by Desulfovibrio vulgaris Hildenborough.
Sulfate-reducing bacteria, like Desulfovibrio vulgaris Hildenborough, use the reduction of sulfate as a sink for electrons liberated in oxidation reactions of organic substrates. The rate of the latter exceeds that of sulfate reduction at the onset of growth, causing a temporary accumulation of hydrogen and other fermentation products (the hydrogen or fermentation burst). In addition to hydroge...
متن کاملExploring the role of CheA3 in Desulfovibrio vulgaris Hildenborough motility
Sulfate-reducing bacteria such as Desulfovibrio vulgaris Hildenborough are often found in environments with limiting growth nutrients. Using lactate as the electron donor and carbon source, and sulfate as the electron acceptor, wild type D. vulgaris shows motility on soft agar plates. We evaluated this phenotype with mutants resulting from insertional inactivation of genes potentially related t...
متن کاملOxygen-dependent growth of the obligate anaerobe Desulfovibrio vulgaris Hildenborough.
Desulfovibrio vulgaris Hildenborough, a sulfate-reducing bacterium classified as an obligate anaerobe, swam to a preferred oxygen concentration of 0.02 to 0.04% (0.24 to 0.48 microM), a level which also supported growth. Oxygen concentrations of 0.08% and higher arrested growth. We propose that in zones of transition from an oxic to an anoxic environment, D. vulgaris protects anoxic microenviro...
متن کاملRedox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough).
The periplasmic Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) contains three iron-sulfur prosthetic groups: two putative electron transferring [4Fe-4S] ferredoxin-like cubanes (two F-clusters), and one putative Fe/S supercluster redox catalyst (one H-cluster). Combined elemental analysis by proton-induced X-ray emission, inductively coupled plasma mass spectrometry, instrumental ne...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1993
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.175.15.4699-4711.1993