Results 211 to 220 of about 9,785 (234)

Purification and properties of cytochrome c3 of desulfovibrio vulgaris, miyazaki

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 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
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Studies on sulfite reduction by Desulfovibrio vulgaris.

Acta microbiologica Polonica, 1982
Dissimilatory 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
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Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough

2018
The [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, Marisela, Vélez, Marcos, Pita, Antonio L, De Lacey, Pedro M, Matias, Inês A C, Pereira   +5 more
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Studies on thiosulfate reduction by Desulfovibrio vulgaris.

Acta microbiologica Polonica, 2009
Dissimilatory 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
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Magnetic susceptibility of hydrogenase from Desulfovibrio vulgaris.

Journal of biochemistry, 1985
Magnetization 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, H, Inokuchi, H, Nanami, T, Yagi   +3 more
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Formate: Cytochrome Oxidoreductase of Desulfovibrio vulgaris

The Journal of Biochemistry, 1969
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Assignment of the redox potentials to the four haems inDesulfovibrio vulgariscytochromec3by 2D-NMR

FEBS Letters, 1992
Carlos A Salgueiro, Helena Santos, J Legall   +2 more
exaly  

The effect of re-oxidation on the reduced hydrogenase of Desulfovibrio vulgaris strain Hildenborough and its oxygen stability

FEBS Letters, 1983
Cees van Dijk, Cees Veeger
exaly  

Structure of a CRISPR-associated protein Cas2 fromDesulfovibrio vulgaris

Acta Crystallographica Section F: Structural Biology Communications, 2010
Paul Smith, Stewart Shuman
exaly  

Utilization of α-glycerophosphate by Desulfovibrio vulgaris

FEMS Microbiology Letters, 1979
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