Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22.
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 (betadelta) and an NADH:acceptor oxidoreductase (alphagamma)], 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.
Grzeszik
C
C
Institut für Mikrobiologie, Georg-August-Universität Göttingen, Grisebachstrasse 8, D-37077 Göttingen, Germany.
Ross
K
K
Schneider
K
K
Reh
M
M
Schlegel
H G
HG
D000421:Alcaligenes / Q000201:enzymology*; D015153:Blotting, Western; D002457:Cell Extracts / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D009532:Nickel / Q000378:metabolism; D010088:Oxidoreductases / Q000032:analysis* / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D011487:Protein Conformation; D012240:Rhodococcus / Q000201:enzymology*
D002457:Cell Extracts; D009532:Nickel; D010088:Oxidoreductases; C021376:hydrogen dehydrogenase