Kinetic study of the enzyme NADPH cytochrome-C (P-450) reductase: non-Michaelian behaviour.
1. Contrary to what has been accepted until now, the enzyme exhibits non-Michaelian kinetics both against NADPH and against cytochrome-c as substrates; deviations were detected that have led to the proposition of a rate equation of minimum degree 2:2. 2. A general mechanism is proposed that includes, apart from the binding of the enzyme to NADPH, the formation of an enzyme-cytochrome-c complex, both routes leading to the formation of a ternary-complex NADPH-enzyme-acceptor. 3. From the latter, a series of intermediate steps finally leads to the release of the enzyme in conditions to start a new catalytic cycle. 4. Application of the King-Altman method to this mechanism yields a kinetic equation of degree 2:2 with respect to the cytochrome-c and NADPH, in accordance with our experimental results.
D000818:Animals; D007700:Kinetics; D008433:Mathematics; D008862:Microsomes, Liver / Q000201:enzymology; D008962:Models, Theoretical; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D009251:NADPH-Ferrihemoprotein Reductase