Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas

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Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas.

A novel adenylate kinase (AK) has recently been purified from Desulfovibrio gigas and characterized as a Co(2+)/Zn(2+)-containing enzyme: this is an unusual characteristic for AKs from Gram-negative bacteria, in which these enzymes are normally devoid of metals. Here, we studied the conformational stability of holo- and apo-AK as a function of temperature by differential scanning calorimetry (D...

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Energy coupling to nitrite respiration in the sulfate-reducing bacterium Desulfovibrio gigas.

By use of a membrane fraction prepared from Desulfovibrio gigas grown in a lactate-sulfate medium, synthesis of ATP was demonstrated to be coupled to the oxidation of molecular hydrogen and reduction of either nitrite or hydroxylamine. This phosphorylation was uncoupled from electron transport by pentachlorophenol, methyl viologen, and gramicidin, but not by oligomycin. The extrusion of protons...

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Isolation of sulfate-reducing bacteria from Tunisian marine sediments and description of Desulfovibrio bizertensis sp. nov.

Several strains of sulfate-reducing bacteria were isolated from marine sediments recovered near Tunis, Korbous and Bizerte, Tunisia. They all showed characteristics consistent with members of the genus Desulfovibrio. One of these strains, designated MB3(T), was characterized further. Cells of strain MB3(T) were slender, curved, vibrio-shaped, motile, Gram-negative, non-spore-forming rods. They ...

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Genome sequence of the model sulfate reducer Desulfovibrio gigas: a comparative analysis within the Desulfovibrio genus*

Desulfovibrio gigas is a model organism of sulfate-reducing bacteria of which energy metabolism and stress response have been extensively studied. The complete genomic context of this organism was however, not yet available. The sequencing of the D. gigas genome provides insights into the integrated network of energy conserving complexes and structures present in this bacterium. Comparison with...

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ژورنال

عنوان ژورنال: Biophysical Chemistry

سال: 2004

ISSN: 0301-4622

DOI: 10.1016/j.bpc.2004.01.006