Evidence for a fourth hydrogenase in Desulfovibrio fructosovorans.
A strain devoid of the three hydrogenases characterized for Desulfovibrio fructosovorans was constructed using marker exchange mutagenesis. As expected, the H(2)-dependent methyl viologen reduction activity of the strain was null, but physiological studies showed no striking differences between the mutated and wild-type strains. The H(+)-D(2) exchange activity measured in the mutated strain indicates the presence of a fourth hydrogenase in D. fructosovorans.
Casalot
Laurence
L
Laboratoire de Bioénergétique et Ingénierie des Protéines, UPR 9036-CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 09, France.
De Luca
Gilles
G
Dermoun
Zorah
Z
Rousset
Marc
M
de Philip
Pascale
P
D001426:Bacterial Proteins; D003901:Desulfovibrio / Q000201:enzymology* / Q000235:genetics; D003903:Deuterium; D006864:Hydrogenase / Q000235:genetics / Q000302:isolation & purification*; D007506:Iron-Sulfur Proteins / Q000235:genetics; D016296:Mutagenesis; D010088:Oxidoreductases / Q000235:genetics; D010269:Paraquat / Q000378:metabolism
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D003903:Deuterium; D010088:Oxidoreductases; C118830:iron hydrogenase; C043296:nickel-iron hydrogenase; C093595:NADP-reducing hydrogenase, Desulfovibrio fructosovorans; D006864:Hydrogenase; D010269:Paraquat