Results 201 to 210 of about 9,790 (220)
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Physicochemical properties of flavodoxin from Desulfovibrio vulgaris
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1975Reductive 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, 2006Biological 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 +4 more
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Guanylcobamide and hypoxanthylcobamide-Corrinoids formed by Desulfovibrio vulgaris
Archives of Microbiology, 1994The corrinoids synthesized by the sulfate-reducing bacterium Desulfovibrio vulgaris were analyzed. The compounds found were guanylcobamide and hypoxanthylcobamide; structures were determined by mass spectrometry, 1H-NMR, and ultraviolet/visible spectroscopy. D.
Daniel Harald Guimar�es +4 more
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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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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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Carbon starvation considerably accelerated nickel corrosion by Desulfovibrio vulgaris
Bioelectrochemistry, 2023Carbon starvation can affect the activity of microbes, thereby affecting the metabolism and the extracellular electron transfer (EET) process of biofilm. In the present work, the microbiologically influenced corrosion (MIC) behavior of nickel (Ni) was investigated under organic carbon starvation by Desulfovibrio vulgaris. Starved D.
Yanan Pu +4 more
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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+
Francesco Bonomi +2 more
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Characterization of Periplasmic Hydrogenase from Desulfovibrio vulgaris Miyazaki K
Journal of Biochemistry, 1983Periplasmic hydrogenase [hydrogen:ferricytochrome c3 oxidoreductase, EC 1.12.2.1] from Desulfovibrio vulgaris Miyazaki K (MK) was purified to homogeneity. Its chemical and immunological properties were examined and compared with those of other Desulfovibrio hydrogenases.
J, Aketagawa, K, Kobayashi, M, Ishimoto
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Crystallographic Study of Cytochrome c553 from Desulfovibrio vulgaris Miyazaki
The Journal of Biochemistry, 1986Cytochrome c553 from the sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki, has been crystallized. The combination of microdialysis and vapor diffusion allowed successful crystallization. The crystals were of good quality, and useful data were obtained that extended to the nominal resolution of 1.3 A.
A, Nakagawa +8 more
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D-lactate dehydrogenase of Desulfovibrio vulgaris.
Journal of biochemistry, 1981D-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
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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 ...
Sónia, Zacarias +5 more
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