Summary: NAD(P)H nitrate reductase (EC from the yeast has been purified to electrophoretic homogeneity. The concentrated enzyme has a molecular mass of 365 kDa and consists of four subunits each of 95 kDa, but appears to dissociate into dimers after dilution. The absorption spectrum of the homogeneous protein is typical of a -type cytochrome and its isoelectric point is pH 5·4. The enzyme utilizes both NADH and NADPH but is more active with NADH. Preincubation of pure enzyme with NAD(P)H and cyanide, but not NAD(P)H and ADP, leads to a reversible redox inactivation of the enzyme. Preincubation with NAD(P)H alone activates the enzyme.


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