NADPH---hemoprotein reductase;
CPR;
FAD-cytochrome c reductase;
NADP---cytochrome c reductase;
NADP---cytochrome reductase;
NADPH-dependent cytochrome c reductase;
NADPH:P-450 reductase;
NADPH:ferrihemoprotein oxidoreductase;
NADPH---cytochrome P-450 oxidoreductase;
NADPH---cytochrome c oxidoreductase;
NADPH---cytochrome c reductase;
NADPH---cytochrome p-450 reductase;
NADPH---ferricytochrome c oxidoreductase;
NADPH---ferrihemoprotein reductase;
TPNH2 cytochrome c reductase;
TPNH-cytochrome c reductase;
aldehyde reductase (NADPH-dependent);
cytochrome P-450 reductase;
cytochrome c reductase (reduced nicotinamide adenine dinucleotide phosphate, NADPH, NADPH-dependent);
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome c reductase;
ferrihemoprotein P-450 reductase;
reduced nicotinamide adenine dinucleotide phosphate-cytochrome c reductase;
reductase, cytochrome c (reduced nicotinamide adenine dinucleotide phosphate)

Oxidoreductases;
Acting on NADH or NADPH;
With a heme protein as acceptor

NADPH:hemoprotein oxidoreductase

NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein

(other) R00106 R05102 R08539 R08551

NADPH [CPD:C00005];
H+ [CPD:C00080];
oxidized hemoprotein

A flavoprotein (FMN, FAD) containing both FMN and FAD. The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. The enzyme catalyses the reduction of the heme-thiolate-dependent monooxygenases, such as EC 1.14.14.1, unspecific monooxygenase and reduction of EC 1.14.99.3, heme oxygenase (decyclizing). It is part of the microsomal hydroxylating system. It also reduces cytochrome b5 and cytochrome c.

1

Haas, E., Horecker, B.L. and Hogness, T.R.

The enzymatic reduction of cytochrome c, cytochrome c reductase.

J. Biol. Chem. 136 (1940) 747-774.

2

Horecker, B.L.

Triphosphopyridine nucleotide-cytochrome c reductase in liver.

J. Biol. Chem. 183 (1950) 593-605.

3  [PMID:4389465]

Lu AY, Junk KW, Coon MJ.

Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components.

J. Biol. Chem. 244 (1969) 3714-21.

Oryctolagus cuniculus

4  [PMID:14275154]

GIBSON QH, PALMER G, WHARTON DC.

STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE.

J. Biol. Chem. 240 (1965) 921-31.

Sus scofa [GN:ssc]

5  [PMID:14007123]

WILLIAMS CH Jr, KAMIN H.

Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver.

J. Biol. Chem. 237 (1962) 587-95.

Sus scofa [GN:ssc]

6  [PMID:4378860]

Masters BS, Bilimoria MH, Kamin H, Gibson QH.

The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase.

J. Biol. Chem. 240 (1965) 4081-8.

Sus scofa [GN:ssc]

7  [PMID:8589067]

Sevrioukova IF, Peterson JA.

NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms.

Biochimie. 77 (1995) 562-72.

Homo sapiens [GN:hsa]

8  [PMID:9237990]

Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ.

Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes.

Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8411-6.

Rattus norvegicus [GN:rno]

9  [PMID:11329262]

Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK.

Determination of the redox properties of human NADPH-cytochrome P450 reductase.

Biochemistry. 40 (2001) 1956-63.

Homo sapiens [GN:hsa], Oryctolagus cuniculus

10 [PMID:12773143]

Gutierrez A, Grunau A, Paine M, Munro AW, Wolf CR, Roberts GC, Scrutton NS.

Electron transfer in human cytochrome P450 reductase.

Biochem. Soc. Trans. 31 (2003) 497-501.

Homo sapiens [GN:hsa]