The presence of multiple intrinsic membrane nickel-containing hydrogenases in Desulfovibrio vulgaris (Hildenborough).
Three intrinsic membrane proteins exhibiting oxygen stable hydrogenase activity have been isolated from D. vulgaris. In contrast to the periplasmic exclusively non-heme iron hydrogenase, all three hydrogenases contain Ni in addition to non-heme iron, have low specific activities and are insensitive to inhibition by CO. None of the three hydrogenases cross react with IgA against the periplasmic hydrogenase of D. vulgaris but two of the new hydrogenases cross react with IgA against the periplasmic nickel containing hydrogenase of D. gigas and the other new hydrogenase cross reacts with IgA against the periplasmic nickel and selenium hydrogenase of D. desulfuricans (Norway -4).
D002248:Carbon Monoxide / Q000494:pharmacology; D003429:Cross Reactions; D003901:Desulfovibrio / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006864:Hydrogenase / Q000032:analysis*; D007070:Immunoglobulin A / Q000276:immunology; D007527:Isoenzymes / Q000032:analysis; D008566:Membranes / Q000201:enzymology; D009532:Nickel / Q000032:analysis*
D007070:Immunoglobulin A; D007527:Isoenzymes; D009532:Nickel; D002248:Carbon Monoxide; D006864:Hydrogenase