Le cytochrome c3 de Desulfovibrio gigas

Gall, Jean Le; Mazza, Gilbert; Dragoni, Nicole

doi:10.1016/s0926-6593(65)80141-2

Cited by 166 publications

(68 citation statements)

References 4 publications

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“…Bacterial strain, culture media, and growth conditions D. desulfuricans ATCC 27774, D. gigas NCIB 9332, and Desulfovibrio alaskensis cells were, respectively, grown in lactate-nitrate [17], lactate-sulfate [18], and in a modified medium C from Postgate [19]. Cells were grown under anaerobic conditions at 37°C and collected by centrifugation at the end of the exponential phase.…”

Section: Methodsmentioning

confidence: 99%

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

et al. 2011

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Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C-H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results.

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Section: Methodsmentioning

confidence: 99%

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

et al. 2011

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“…Several types of cytochromes of the b or c types have been isolated from them. D. gigas contains at least five different cytochromes: cytochrome b [l], tetraheme cytochrome cr [2], octaheme cytochrome c3 [3], a partially identified membrane-bound cytochrome c [4], and a new type of flavohemo protein, a rubredoxin-oxygen oxidoreductase [5].…”

Section: Lntroduetionmentioning

confidence: 99%

Isolation and characterization of a high molecular weight cytochrome from the sulfate reducing bacterium Desulfovibrio gigas

et al. 1994

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A high molecular weight c-type cytochrome (Hmc) was purified and characterized from Desulfovibrio gigas. The molecular weight was estimated to be 67 kDa by SDS-PAGE and its N-terminus is homologous to those of the 16 hemes containing high molecular weight cytochrome c from Desulfovibrio vulgaris strains Hildenborough and Miyaxaki. The purified hemoprotein shows c-type cytochrome absorption spectrum with s,,,(red) = 368 mM-' . cm-'. A band at 640 nm, characteristic of high-spin hemes, was detected The EPR spectra show the presence of two high-spin heme species, plus several non-equivalent low-spin hemes. The heme reduction potentials, at pH 7.6, range from -50 mV to -315 mV. In contrast to what has been described for D. vulgaris Hmc, the protein isolated from D. gigas directly accepts electrons from hydrogenase and further reduces other redox proteins.

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“…The purification procedure of native D. vulgaris cytochrome c551 from D. desuljuricans G200 was previoudy reported (Blanchard et al, 1993 350 g wet cells were obtained from 300 1 fermentation in Postgate medium C supplemented with 0.28 mM kanamycin and were harvested as previously described (LeGall et al, 1965). The mutants.…”

Section: Purification Of Recombinant and Mutant Cytochromes Css3 Overmentioning

confidence: 99%

Effects of the Tyr64 Substitution on the Stability of Cytochrome c₅₅₃, a low Oxidoreduction‐Potential Cytochrome from Desulfovibrio vulgaris Hildenborough

Blanchard

Dolla

Bersch

et al. 1994

European Journal of Biochemistry

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Cytochrome c553 from sulfate‐reducing bacteria is a lowoxidoreduction‐potential cytochrome. The primary and tertiary structures show notable differences when compared to mitochondrial cytochromes. Tyr64 replacement in cytochrome c553 provides evidence that this residue is not directly involved in the potential modulation but is mostly implicated in the hydrogenbond network around the heme. While the different variants obtained did not induce drastic structural modifications, they did affect the stability of the protein. This decrease of stability in acidic and alkaline environments was observed by variations in the optical spectra and by mass spectrometry. In addition, the mobility of aromatic side‐chain was found to be increased in the mutant proteins as monitored by two‐dimensional NMR spectroscopy.

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Le cytochrome c3 de Desulfovibrio gigas

Cited by 166 publications

References 4 publications

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

Isolation and characterization of a high molecular weight cytochrome from the sulfate reducing bacterium Desulfovibrio gigas

Effects of the Tyr64 Substitution on the Stability of Cytochrome c₅₅₃, a low Oxidoreduction‐Potential Cytochrome from Desulfovibrio vulgaris Hildenborough

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Le cytochrome c3 de Desulfovibrio gigas

Cited by 166 publications

References 4 publications

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

Isolation and characterization of a high molecular weight cytochrome from the sulfate reducing bacterium Desulfovibrio gigas

Effects of the Tyr64 Substitution on the Stability of Cytochrome c553, a low Oxidoreduction‐Potential Cytochrome from Desulfovibrio vulgaris Hildenborough

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Effects of the Tyr64 Substitution on the Stability of Cytochrome c₅₅₃, a low Oxidoreduction‐Potential Cytochrome from Desulfovibrio vulgaris Hildenborough