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KMID : 0380219940270030201
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 3 p.201 ~ p.204
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Enzymatic Properties of Two Distinct NADH Oxidases in the Respiratory Chain of the Marine Bacterium Vibrio alginolyticus
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Abstract
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Abstract:
@EN Two kinds of NADH oxidases were isolated from the respiratory chain of Vibrio olginolyticus in order to study their enzymatic properties. Wild type membranes, which possess NADH: quinone reductase 2 (NQR2), as well as NADH: quinone reductase
1
(NQR1), oxidized both NADH and deamino-NADH as substrates. Membranes of a mutant bacterium defective in the Na pump (Nap1), which contain only NQR2, oxidized NADH exclusively. Compared with NQR1 the reductase activity of NQR2 for artificial
electron
acceptors in the presence of NADH or deamino-NADH was relatively low. These two reductases have different specificities for electron acceptor. Wild type membranes exhibited two apparent Km values for NADH, 5 to 8 μM and 25 to 30 μM. Napl
membranes
exhibited only a single apparent Km value of 27 to 35 μM for NADH. The two kinds of NADH oxidase in the V. alginolyticus respiratory chain apparently differ considerably in their enzymatic properties.
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