Iron (III) reduction: A novel activity of the human NAD(P)H:oxidoreductase.
NAD(P)H:quinone oxidoreductase (NQO1; EC 1.6.99.2) catalyzes a two-electron transfer involved in the protection of cells from reactive oxygen species. These reactive oxygen species are often generated by the one-electron reduction of quinones or quinone analogs. We report here on the previously unreported Fe(III) reduction activity of human NQO1. Under steady state conditions with Fe(III) citrate, the apparent Michaelis-Menten constant (Km(app)) was approximately 0.3 nM and the apparent maximum velocity (Vmax(app)) was 16 U mg(-1). Substrate inhibition was observed above 5 nM. NADH was the electron donor, Km(app)= 340 microM and Vmax(app) = 46 Umg(-1). FAD was also a cofactor with a Km(app) of 3.1 microM and Vmax(app) of 89 U mg(-1). The turnover number for NADH oxidation was 25 s(-1). Possible physiological roles of the Fe(III) reduction by this enzyme are discussed.
Onyenwoke
Rob U
RU
Department of Microbiology, The University of Georgia, 1000 Cedar Street, Athens, GA 30602-2605, USA.
Wiegel
Juergen
J
D002384:Catalysis; D004789:Enzyme Activation; D006801:Humans; D007501:Iron / Q000737:chemistry*; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry*; D010084:Oxidation-Reduction; D013379:Substrate Specificity
D007501:Iron; D016660:NAD(P)H Dehydrogenase (Quinone); C447479:NQO1 protein, human