Results 201 to 210 of about 9,785 (234)

Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris

Applied and Environmental Microbiology, 1993
The mechanism for U(VI) reduction by Desulfovibrio vulgaris (Hildenborough) was investigated. The H2-dependent U(VI) reductase activity in the soluble fraction of the cells was lost when the soluble fraction was passed over a cationic exchange column which extracted cytochrome c3.
Lovley, Derek, Widman, Peggy K, Woodward, Joan C, Philips, Elizabeth J.P   +3 more
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Physicochemical properties of flavodoxin from Desulfovibrio vulgaris

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
Reductive titration curves of flavodoxin from Desulfovibrio vulgaris displayed two one-electron steps. The redox potential E-2 for the couple oxidized flavodoxin/flavodoxin semiquinone was determined by direct titration with dithionite. E-2 was -149 plus or minus 3 mV (pH 7.78, 25 degrees C).
M, Dubourdieu, J, le Gall, V, Favaudon
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Toxic effects of dissolved heavy metals on Desulfovibrio vulgaris and Desulfovibrio sp. strains

Journal of Hazardous Materials, 2006
Biological treatment of metal-containing wastewaters with sulphate-reducing bacteria (SRB) is an attractive technique for the bioremediation of this kind of medium. In order to design a suitable engineering process to address this environmental problem, it is crucial to understand the inhibitory effect of dissolved heavy metals on these bacteria. Batch
G, Cabrera, R, Pérez, J M, Gómez, A, Abalos, D, Cantero   +4 more
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Membrane protein complex of APS reductase and Qmo is present in Desulfovibrio vulgaris and Desulfovibrio alaskensis

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.
Lee R, Krumholz, Luyao, Wang, David A C, Beck, Tiansong, Wang, Murray, Hackett, Brian, Mooney, Thomas R, Juba, Michael J, McInerney, Birte, Meyer, Judy D, Wall, David A, Stahl   +10 more
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Generation of a proton gradient in Desulfovibrio vulgaris

Archives of Microbiology, 1991
Washed cells of Desulfovibrio vulgaris strain Marburg oxidized H2, formate, lactate or pyruvate with sulfate, sulfite, trithionate, thiosulfate or oxygen as electron acceptor. CuCl2 as an inhibitor of periplasmic hydrogenase inhibited H2 and formate oxidation with sulfur compounds, and lactate oxidation in H2-grown, but not in lactate-grown cells.
Robert M. Fitz, Heribert Cypionka
openaire   +1 more source

Octomeric pyruvate-ferredoxin oxidoreductase from Desulfovibrio vulgaris

Journal of Structural Biology, 2007
Pyruvate-ferredoxin oxidoreductatse (PFOR) carries out the central step in oxidative decarboxylation of pyruvate to acetyl-CoA. We have purified this enzyme from Desulfovibrio vulgaris Hildenborough (DvH) as part of a systematic characterization of as many multiprotein complexes as possible for this organism, and the three-dimensional structure of this
Florian, Garczarek, Ming, Dong, Dieter, Typke, H Ewa, Witkowska, Terry C, Hazen, Eva, Nogales, Mark D, Biggin, Robert M, Glaeser   +7 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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Some observations on growth and hydrogen uptake by Desulfovibrio vulgaris

Archiv f�r Mikrobiologie, 1971
1. Calculation showed that rates of sulphate reduction by the Hildenborough strain of Desulfovibrio vulgaris in non-nutrient buffer with gaseous hydrogen as electron donor were as high as, or higher than, the maximum possible rate of sulphate reduction during growth. 2.
B, Khosrovi, R, Macpherson, J D, Miller
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D-lactate dehydrogenase of Desulfovibrio vulgaris.

Journal of biochemistry, 1981
D-Lactate dehydrogenase, the starting enzyme for carbon and energy metabolism in dissimilatory sulfate-reducing bacteria, has been purified 36-fold from the soluble fraction of the sonicate of Desulfovibrio vulgaris, Miyazaki. The enzyme is specific for D-lactate (Km = 0.8 mM) and DL-2-hydroxybutyrate (probably its D-isomer) as the electron donor ...
M, Ogata, K, Arihara, T, Yagi
openaire   +1 more source

Ferroxidase activity of recombinant Desulfovibrio vulgaris rubrerythrin

JBIC Journal of Biological Inorganic Chemistry, 1996
Rubrerythrin (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+
Francesco Bonomi, D. M. Kurtz, Xiaoyuan Cui   +2 more
openaire   +1 more source