POR reduces CYP450:Fe3+ to CYP450:Fe2+

Stable Identifier
Reaction [transition]
Homo sapiens
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NADPH-cytochrome P450 reductase (POR) (Shephard et al. 1992) and cytochrome-b5 and NADH-b5 reductase play important roles in cytochrome P450-mediated drug metabolism (Gan et al. 2009). POR can transfer electrons to many naturally occurring electron acceptors, including cytochrome P450 enzymes where it transfers the electrons from NADPH into the P450 catalytic cycle (Elmore & Porter 2002). The P450 catalytic cycle describes the transitional mechanistic steps by which P450s bind a substrate, act upon it and finally release the product, returning P450s to their initial state (see mini-review Guengerich 2007).

Literature References
PubMed ID Title Journal Year
17936929 Mechanisms of cytochrome P450 substrate oxidation: MiniReview

Guengerich, FP

J. Biochem. Mol. Toxicol. 2007
18838505 Role of NADPH-cytochrome P450 reductase and cytochrome-b5/NADH-b5 reductase in variability of CYP3A activity in human liver microsomes

Trepanier, LA, Court, MH, von Moltke, LL, Harmatz, JS, Gan, L, Greenblatt, DJ

Drug Metab. Dispos. 2009
12381719 Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in Vivo

Porter, TD, Elmore, CL

J. Biol. Chem. 2002
1550342 Quantification of cytochrome P450 reductase gene expression in human tissues

Segall, HJ, Palmer, CN, Shephard, EA, Phillips, IR

Arch. Biochem. Biophys. 1992
Event Information
Catalyst Activity

NADPH-hemoprotein reductase activity of POR [endoplasmic reticulum membrane]

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