Cytoplasmic nickel-iron hydrogenase with high specific activity from Desulfovibrio multispirans sp. N. , a new species of sulfate reducing bacterium

Journal Article · Fri Dec 28 00:00:00 EST 1984 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/0006-291X(84)91386-X· OSTI ID:6055524

Czechowski, M H; He, S H; Nacro, M; DerVartanian, D V; Peck, Jr, H D; LeGall, J

A hydrogenase from a new species of sulfate reducing bacterium has been isolated and characterized. In contrast to other hydrogenases isolated from Desulfovibrio, this enzyme is found in the cytoplasmic fraction rather than in the periplasm. The specific activity of the enzyme, as measured in the hydrogen evolution assay, is twice as high as the specific activity of the hydrogenase from D. gigas. It also differentiates itself from the periplasmic Desulfovibrio hydrogenases by being more active in the hydrogen evolution rather than in the hydrogen uptake assay. The enzyme was shown to contain 0.9 atoms of nickel, 11 atoms of iron and 10 atoms of labile sulfide per mole of enzyme. It exhibits an unusually low intensity of the g = 2.31 nickel EPR signal in the isolated enzyme but shows a normal intensity for the g = 2.19 nickel EPR signal when reduced under hydrogen.

• Research Organization: Univ. of Georgia, Athens
• DOE Contract Number: AS09-79ER10499
• OSTI ID: 6055524
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Vol. 125:3
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
DESULFOVIBRIO
BIOCHEMISTRY
HYDROGENASES
ENZYME ACTIVITY
STRUCTURAL CHEMICAL ANALYSIS
CYTOPLASM
ELECTRON SPIN RESONANCE
IRON
NICKEL
SULFIDES
BACTERIA
CELL CONSTITUENTS
CHALCOGENIDES
CHEMISTRY
ELEMENTS
ENZYMES
MAGNETIC RESONANCE
METALS
MICROORGANISMS
OXIDOREDUCTASES
RESONANCE
SULFATE-REDUCING BACTERIA
SULFUR COMPOUNDS
TRANSITION ELEMENTS
550700* - Microbiology