Sulfate‐reducing microorganisms extensively contribute to the corrosion of ferrous metal infrastructure. There is substantial debate over their corrosion mechanisms.
Di Wang +4 more
doaj +1 more source
Deletion Mutants, Archived Transposon Library, and Tagged Protein Constructs of the Model Sulfate-Reducing Bacterium Desulfovibrio vulgaris Hildenborough. [PDF]
Wall JD +13 more
europepmc +1 more source
Carbon 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.
Voordouw, G.
core
Characterization of the Desulfovibrio vulgaris Hildenborough small RNA SIC2
Desulfovibrio vulgaris Hildenborough (DvH) is a gram-negative, anaerobic, sulfate-reducing bacterium (SRB). SRB are capable of using sulfate as a terminal electron acceptor resulting in the production of hydrogen sulfide as an end product.
Miller, Jeremiah Samuel
core
Experimental evolution reveals nitrate tolerance mechanisms in Desulfovibrio vulgaris. [PDF]
Wu B +16 more
europepmc +1 more source
Virtual screening and molecular dynamic simulations of <i>Desulfovibrio vulgaris</i> dissimilatory sulfite reductase inhibitors for the control of sulphate reducing bacteria. [PDF]
Oyewole OA +6 more
europepmc +1 more source
Absence of biofilm adhesin proteins changes surface attachment and cell strategy for Desulfovibrio vulgaris Hildenborough. [PDF]
Pickens CP, Wang D, Pan C, De León KB.
europepmc +1 more source
The physiological role of the cytoplasmic hydrogenases in Desulfovibrio vulgaris
The Gram-negative Deltaproteobacterium D. vulgaris Hildenborough is able to grow with sulfate, sulfite and thiosulfate as electron acceptors and in their absence via fermentation or syntrophic association with hydrogenotrophic organisms. Despite decades of research, the mechanism of energy generation by D. vulgaris is not well understood.
Stolyar, S. +4 more
openaire +1 more source
Directed evolution of an ultrastable carbonic anhydrase from <i>Desulfovibrio vulgaris</i> towards enhanced tolerance to flue gas impurities. [PDF]
Antonopoulou I +5 more
europepmc +1 more source
The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in <i>Desulfovibrio vulgaris</i> Ni-Fe Carbon Monoxide Dehydrogenase. [PDF]
Wittenborn EC +7 more
europepmc +1 more source

