Results 1 to 10 of about 4,354 (194)
Assignment of the redox potentials to the four haems inDesulfovibrio vulgariscytochromec3by 2D-NMR
FEBS Letters, 1992 Using 2D-NMR the four haems of Desulfovibrio vulgaris (Hildenborough) cytochromes, within the X-ray structure were fully cross-assigned according to their redox potential.
CARLOS A Salgueiro +2 more
exaly +2 more sources
Some of the next articles are maybe not open access.
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
openaire +1 more source
Purification and properties of cytochrome c3 of desulfovibrio vulgaris, miyazaki
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract Cytochrome c 3 was isolated in a homogenous state from Desulfovibrio vulgaris , Miyazaki, and its properties examined and compared with those of the cytochrome c 3 from D. vulgaris , Hildenborough. The absorption spectrum of the ultraviolet region of ferrocytochrome c 3 was recorded for the first time.
T, Yagi, K, Maruyama
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+
Francesco Bonomi +2 more
openaire +1 more source
Studies on sulfite reduction by Desulfovibrio vulgaris.
Acta microbiologica Polonica, 1982Dissimilatory reduction of sulfites by Desulfovibrio vulgaris was investigated. Medium with alpha-glycerophosphate as a source of organic carbon and phosphorus was applied. It was found that sulfite at the concentration up to 1M Na2SO3 is not toxic for D. vulgaris and acts efficiently as an electron acceptor.
F, Domka, M, Szulczyński
openaire +1 more source
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
openaire +2 more sources
Studies on thiosulfate reduction by Desulfovibrio vulgaris.
Acta microbiologica Polonica, 2009Dissimilatory reduction of thiosulfate in a-glycerophosphate, lactate and pyruvate media has been studied. Simplified equations describing respiration of bacteria have been proposed on the ground of the established stoichiometry of the reduction process.
F, Domka, M, Szulczyński
openaire +1 more source
Formate: Cytochrome Oxidoreductase of Desulfovibrio vulgaris
The Journal of Biochemistry, 1969openaire +2 more sources
Magnetic susceptibility of hydrogenase from Desulfovibrio vulgaris.
Journal of biochemistry, 1985Magnetization and magnetic susceptibility measurements revealed that the hydrogenase [EC 1.12.2.1] from Desulfovibrio vulgaris Miyazaki F has an independent unpaired electron in its iron-sulfur cluster. The paramagnetic center of the Desulfovibrio hydrogenase is, therefore, different from that in the Chromatium hydrogenase which interacts with another ...
K, Kimura +3 more
openaire +1 more source