Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22 |
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Authors: | C. Grzeszik K. Roß K. Schneider M. Reh H. G. Schlegel |
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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
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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 |
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Keywords: | Soluble NAD-reducing hydrogenase Membrane-bound hydrogenase Diaphorase Rhodococcus opacus 1b Alcaligenes eutrophus H16 |
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