Results 31 to 40 of about 112,078 (164)

Response of Desulfovibrio vulgaris Hildenborough to Acid pH [PDF]

open access: yes, 2007
The anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough has been suggested to be useful for environmental bioremediation applications.
Wall, J.D.
core   +2 more sources

Linking NrfD/PsrC-like architecture to energy conservation: Functional residues in the quinone reactive QrcABCD complex of sulfate-reducing bacteria. [PDF]

open access: yesProtein Sci
Abstract The QrcABCD quinone reductase complex is an electrogenic complex present in sulfate‐reducing bacteria of the Desulfobacterota phylum. It operates as a cytochrome c3:menaquinone oxidoreductase involved in electron transfer from periplasmic hydrogen or formate oxidation to the menaquinone (MK) pool.
Manteigas G   +4 more
europepmc   +2 more sources

Purification, crystallization and preliminary crystallographic analysis of the [NiFeSe] hydrogenase fromDesulfovibrio vulgarisHildenborough [PDF]

open access: yesActa Crystallographica Section F: Structural Biology Communications, 2009
Pedro M Matias   +2 more
exaly   +2 more sources

Genetic Basis of Chromate Adaptation and the Role of the Pre-existing Genetic Divergence during an Experimental Evolution Study with Desulfovibrio vulgaris Populations

open access: yesmSystems, 2021
Hexavalent chromium [Cr(VI)] is a common environmental pollutant. However, little is known about the genetic basis of microbial evolution under Cr(VI) stress and the influence of the prior evolution histories on the subsequent evolution under Cr(VI ...
Weiling Shi   +9 more
doaj   +1 more source

Carboxysome‐Inspired Electrocatalysis using Enzymes for the Reduction of CO2 at Low Concentrations**

open access: yesAngewandte Chemie, Volume 135, Issue 26, June 26, 2023., 2023
A bioinspired approach using enzyme electrocatalysis for the efficient direct reduction of CO2 at low concentrations to formate using Carbonic Anhydrase co‐immobilized with Formate Dehydrogenase in a mesoporous indium tin oxide electrode is described. Abstract The electrolysis of dilute CO2 streams suffers from low concentrations of dissolved substrate
Samuel J. Cobb   +4 more
wiley   +2 more sources

Regulation of Nitrite Stress Response in Desulfovibrio vulgaris Hildenborough, a Model Sulfate-Reducing Bacterium. [PDF]

open access: yesJ Bacteriol, 2015
Sulfate-reducing bacteria (SRB) are sensitive to low concentrations of nitrite, and nitrite has been used to control SRB-related biofouling in oil fields.
Rajeev L   +7 more
europepmc   +2 more sources

Rex (encoded by DVU_0916) in Desulfovibrio vulgaris Hildenborough is a repressor of sulfate adenylyl transferase and is regulated by NADH. [PDF]

open access: yesJ Bacteriol, 2015
Although the enzymes for dissimilatory sulfate reduction by microbes have been studied, the mechanisms for transcriptional regulation of the encoding genes remain unknown. In a number of bacteria the transcriptional regulator Rex has been shown to play a
Christensen GA   +8 more
europepmc   +2 more sources

A rubrerythrin operon and nigerythrin gene in Desulfovibrio vulgaris (Hildenborough) [PDF]

open access: yesJournal of Bacteriology, 1997
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 ...
H L, Lumppio   +4 more
openaire   +2 more sources

Isotopic Fractionation Associated With Sulfate Import and Activation by Desulfovibrio vulgaris str. Hildenborough

open access: yesFrontiers in Microbiology, 2020
The use of stable isotopes to trace biogeochemical sulfur cycling relies on an understanding of how isotopic fractionation is imposed by metabolic networks.
Derek A. Smith   +4 more
doaj   +1 more source

Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species [PDF]

open access: yes, 1988
The localization of APS reductase and bisulfite reductase in Desulfovibrio gigas, D. vulgaris Hildenborough and D. thermophilus was studied by immunoelectron microscopy.
Moura, J.J.G.   +23 more
core   +2 more sources

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