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• W2008575230 abstract "ABSTRACT The physiological properties of a hyd mutant of Desulfovibrio vulgaris Hildenborough, lacking periplasmic Fe-only hydrogenase, have been compared with those of the wild-type strain. Fe-only hydrogenase is the main hydrogenase of D. vulgaris Hildenborough, which also has periplasmic NiFe- and NiFeSe-hydrogenases. The hyd mutant grew less well than the wild-type strain in media with sulfate as the electron acceptor and H 2 as the sole electron donor, especially at a high sulfate concentration. Although the hyd mutation had little effect on growth with lactate as the electron donor for sulfate reduction when H 2 was also present, growth in lactate- and sulfate-containing media lacking H 2 was less efficient. The hyd mutant produced, transiently, significant amounts of H 2 under these conditions, which were eventually all used for sulfate reduction. The results do not confirm the essential role proposed elsewhere for Fe-only hydrogenase as a hydrogen-producing enzyme in lactate metabolism (W. A. M. van den Berg, W. M. A. M. van Dongen, and C. Veeger, J. Bacteriol. 173:3688–3694, 1991). This role is more likely played by a membrane-bound, cytoplasmic Ech-hydrogenase homolog, which is indicated by the D. vulgaris genome sequence. The physiological role of periplasmic Fe-only hydrogenase is hydrogen uptake, both when hydrogen is and when lactate is the electron donor for sulfate reduction." @default.
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• W2008575230 date "2002-02-01" @default.
• W2008575230 modified "2023-09-25" @default.
• W2008575230 title "Effects of Deletion of Genes Encoding Fe-Only Hydrogenase of <i>Desulfovibrio vulgaris</i> Hildenborough on Hydrogen and Lactate Metabolism" @default.
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• W2008575230 doi "https://doi.org/10.1128/jb.184.3.679-686.2002" @default.
• W2008575230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/139517" @default.
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