Results 141 to 150 of about 112,078 (164)

Cloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenborough)

Biochemistry, 1991
The gene coding for rubrerythrin from the sulfate-reducing bacterium Desulfovibrio vulgaris (Hildenborough) has been cloned and sequenced. Rubrerythrin is known to contain two types of iron sites: one rubredoxin-like FeS4 center in each of the two identical subunits and one hemerythrin-like diiron site per dimer [LeGall, J., et al.
B C, Prickril, D M, Kurtz, J, LeGall, G, Voordouw   +3 more
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Bacterioferritin protects the anaerobe Desulfovibrio vulgaris Hildenborough against oxygen

Anaerobe, 2012
Intracellular free iron, is under aerobic conditions and via the Fenton reaction a catalyst for the formation of harmful reactive oxygen species. In this article, we analyzed the relation between intracellular iron storage and oxidative stress response in the sulfate reducing bacterium Desulfovibrio vulgaris Hildenborough, an anaerobe that is often ...
Mafalda C O, Figueiredo, Susana A L, Lobo, João N, Carita, Lígia S, Nobre, Lígia M, Saraiva   +4 more
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Function of formate dehydrogenases in Desulfovibrio vulgaris Hildenborough energy metabolism

Microbiology, 2013
The genome of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough encodes three formate dehydrogenases (FDHs), two of which are soluble periplasmic enzymes (FdhAB and FdhABC3) and one that is periplasmic but membrane-associated (FdhM).
Sofia M, da Silva, Johanna, Voordouw, Cristina, Leitão, Mónica, Martins, Gerrit, Voordouw, Inês A C, Pereira   +5 more
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Overexpression, purification and immunodetection of DsrD from Desulfovibrio vulgaris Hildenborough

Antonie van Leeuwenhoek, 2000
Dissimilatory sulfite reductase (DsrAB) of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough is an alpha2beta2 tetramer of 180 kDa, encoded by the dsr operon. In addition to the dsrA and dsrB genes, this operon contains a gene (dsrD) encoding a protein of only 78 amino acids.
D S, Hittel, G, Voordouw
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Genomic Insights into Gene Regulation of Desulfovibrio vulgaris Hildenborough

OMICS: A Journal of Integrative Biology, 2004
Traditional laboratory studies of the sulfate-reducing bacteria have focused primarily on the biochemistry of the organisms. As genomic sequences of sulfate-reducing species have become available, insights have been gained into the metabolic and regulatory networks of these organisms.
Christopher L, Hemme, Judy D, Wall
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Identification of a membrane-bound hydrogenase of Desulfovibrio vulgaris (Hildenborough)

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
Abstract Two hydrogenase activities from Desulfovibrio vulgaris (Hildenborough) could be distinguished immunologically and biochemically. The first activity, described as hydrogenase I, corresponded to the soluble enzyme located in the periplasmic space of D. vulgaris .
Laura A. Gow, Ishverlal P. Pankhania, Stuart P. Ballantine, David H. Boxer, W.Allan Hamilton   +4 more
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Electrode reaction of cytochrome c3from “Desulfovibrio vulgaris” hildenborough and “Desulfovibrio desulfuricans” norway

Journal of Electroanalytical Chemistry and Interfacial Electrochemistry, 1979
Summary Cyclic voltammetry has shown that reduction-reoxidation processesof D. vulgaris Hildenborough and D. desulfuricans Norway cytochromes c 3 correspond to rather fast electronic exchanges. Two steps for the former and three (two of which are very close) for the latter are detected.
P. Bianco, G. Fauque, J. Haladjian
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Construction of a [NiFe]-hydrogenase deletion mutant of Desulfovibrio vulgaris Hildenborough

Biochemical Society Transactions, 2005
A mutant of Desulfovibrio vulgaris Hildenborough lacking a gene for [NiFe] hydrogenase was generated. Growth studies, performed for the mutant in comparison with the wild-type, showed no strong differences during the exponential growth phase. However, the mutant cells died more rapidly in the stationary growth phase.
A, Goenka, J K, Voordouw, W, Lubitz, W, Gärtner, G, Voordouw   +4 more
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Role of the Tetrahemic Subunit in Desulfovibrio vulgaris Hildenborough Formate Dehydrogenase

Biochemistry, 2005
In the anaerobic sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough (DvH), the genome sequencing revealed the presence of three operons encoding formate dehydrogenases. fdh1 encodes an alphabetagamma trimeric enzyme containing 11 heme binding sites; fdh2 corresponds to an alphabetagamma trimeric enzyme with a tetrahemic subunit; fdh3 ...
Latifa, ElAntak, Alain, Dolla, Marie-Claire, Durand, Pierre, Bianco, Françoise, Guerlesquin   +4 more
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Response of Desulfovibrio vulgaris Hildenborough to hydrogen peroxide: enzymatic and transcriptional analyses.

FEMS microbiology letters, 2010
We studied the effect of hydrogen peroxide (H(2)O(2)) stress on the anaerobic sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. In a lactate/sulfate medium, growth was affected from 0.1 mM H(2)O(2) and totally inhibited at 0.7 mM. Surprisingly, transcript analyses revealed that the PerR regulon exhibited opposite regulation in the ...
Brioukhanov, Andrei, Durand, Marie-Claire, Dolla, Alain, Aubert, Corinne   +3 more
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