Results 181 to 190 of about 139,239 (224)
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Microbiology, 2013
Due to their adjacent location in the genomes of Desulfovibrio species and their potential for formation of an electron transfer pathway in sulfate-reducing prokaryotes, adenosyl phosphosulfate (APS) reductase (Apr) and quinone-interacting membrane-bound oxidoreductase (Qmo) have been thought to interact together during the reduction of APS.
Michael J. McInerney +10 more
openaire +3 more sources
Due to their adjacent location in the genomes of Desulfovibrio species and their potential for formation of an electron transfer pathway in sulfate-reducing prokaryotes, adenosyl phosphosulfate (APS) reductase (Apr) and quinone-interacting membrane-bound oxidoreductase (Qmo) have been thought to interact together during the reduction of APS.
Michael J. McInerney +10 more
openaire +3 more sources
Characterization of a butyrate kinase from Desulfovibrio vulgaris str. Hildenborough.
FEMS Microbiology Letters, 2020Short and branched chain fatty acid kinases participate in both bacterial anabolic and catabolic processes, including fermentation, through the reversible, ATP-dependent synthesis of acyl phosphates.
Maxwell J. Bachochin +4 more
semanticscholar +1 more source
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.
G. Fauque, Jean Haladjian, Pierre Bianco
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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.
G. Fauque, Jean Haladjian, Pierre Bianco
openaire +2 more sources
Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin
JBIC Journal of Biological Inorganic Chemistry, 1996Rubrerythrin (Rr) is the trivial name given to a non-heme iron protein of unknown function which has been found in anaerobic sulfate-reducing bacteria. Rr is unique in containing both rubredoxin-type FeS4 and diiron-oxo sites in the same protein. The results described here demonstrate for the recombinant protein that: (a) Rr catalyzes oxidation of Fe2+
Xiaoyuan Cui +2 more
openaire +2 more sources
Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough
2018The [NiFeSe] hydrogenases are a subgroup of the well-characterized family of [NiFe] hydrogenases, in which a selenocysteine is a ligand to the nickel atom in the binuclear NiFe active site instead of cysteine. These enzymes display very interesting catalytic properties for biological hydrogen production and bioelectrochemical applications: high H2 ...
Inês A. C. Pereira +5 more
openaire +3 more sources
Environmental Microbiology, 2019
Microbiologically influenced corrosion causes $100 billion in damage per year, and biofilms formed by sulfate-reducing bacteria (SRB) are the major culprit. However, little is known about the regulation of SRB biofilm formation.
Lei Zhu +4 more
semanticscholar +1 more source
Microbiologically influenced corrosion causes $100 billion in damage per year, and biofilms formed by sulfate-reducing bacteria (SRB) are the major culprit. However, little is known about the regulation of SRB biofilm formation.
Lei Zhu +4 more
semanticscholar +1 more source
Purification and Characterization of Ferredoxin from Desulfovibrio vulgaris Miyazaki1
The Journal of Biochemistry, 1988Two ferredoxins, Fd I and Fd II, were isolated and purified from Desulfovibrio vulgaris Miyazaki. The major component, Fd I, is an iron-sulfur protein of Mr 12,000, composed of two identical subunits. The absorption spectra of Fd I and Fd II have a broad absorption shoulder near 400 nm characteristic of iron-sulfur proteins. The purity index, A400/A280,
Naoko Okawara +3 more
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