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Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22
Authors:C. Grzeszik  K. Roß  K. Schneider  M. Reh  H. G. Schlegel
Affiliation:Institut für Mikrobiologie, Georg-August-Universit?t G?ttingen, Grisebachstrasse 8, D-37077 G?ttingen, Germany Tel. +49-551-393771, Fax +49-551-393793 e-mail hschleg1@gwdg.de, DE
Abstract:Six new strains of Alcaligenes enriched for and isolated as nickel-resistant bacteria resemble Alcaligenes eutrophus H16 and contain both an NAD-reducing, tetrameric soluble hydrogenase and a membrane-bound hydrogenase. None of the soluble hydrogenases share with the Rhodococcus opacus MR11 enzyme tetramer the property of being cleaved easily into two dimeric moieties [a hydrogenase (βδ) and an NADH:acceptor oxidoreductase (αγ)], in the absence of nickel or at low ionic strength. The soluble hydrogenase of the newly isolated strain MR22 of R. opacus equalled that of strain MR11. The absence of a membrane-bound hydrogenase in Alcaligenes denitrificans strain 4a-2 and in Alcaligenes ruhlandii was confirmed. Received: 14 May 1996 / Accepted: 7 November 1996
Keywords:Soluble NAD-reducing hydrogenase  Membrane-bound hydrogenase  Diaphorase  Rhodococcus opacus 1b  Alcaligenes eutrophus H16
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