NADPH—hemoprotein reductase

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NADPH—hemoprotein reductase
1j9z.jpg
NADPH-Cytochrome P450 reductase dimer, Rattus norvegicus
Identifiers
EC number 1.6.2.4
CAS number 9023-03-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a NADPH—hemoprotein reductase (EC 1.6.2.4) is an enzyme that catalyzes the chemical reaction

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

The 3 substrates of this enzyme are NADPH, H+, and oxidized hemoprotein, whereas its two products are NADP+ and reduced hemoprotein.

This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with a heme protein as acceptor. The systematic name of this enzyme class is NADPH:hemoprotein oxidoreductase. Other names in common use include 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, and phosphate). It has 2 cofactors: FAD, and FMN.

Structural studies[edit]

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1AMO, 1B1C, 1J9Z, 1JA0, 1JA1, 1YQO, 1YQP, 2BF4, 2BN4, and 2BPO.

References[edit]

  • Haas E, Horecker BL, Hogness TR (1940). "The enzymatic reduction of cytochrome c, cytochrome c reductase". J. Biol. Chem. 136: 747–774. 
  • Horecker BL (1950). "Triphosphopyridine nucleotide-cytochrome c reductase in liver". J. Biol. Chem. 183: 593–605. 
  • Lu AY, Junk KW, Coon MJ (1969). "Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components". J. Biol. Chem. 244 (13): 3714–21. PMID 4389465. 
  • GIBSON QH, PALMER G, WHARTON DC (1965). "STUDIES ON THE MECHANISM OF MICROSOMAL TRIPHOSPHOPYRIDINE NUCLEOTIDE-CYTOCHROME C REDUCTASE". J. Biol. Chem. 240: 921–31. PMID 14275154. 
  • WILLIAMS CH Jr; KAMIN H (1962). "Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver". J. Biol. Chem. 237: 587–95. PMID 14007123. 
  • Masters BS, Bilimoria MH, Kamin H, Gibson QH (1965). "The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase". J. Biol. Chem. 240 (10): 4081–8. PMID 4378860. 
  • Sevrioukova IF, Peterson JA (1995). "NADPH-P-450 reductase: structural and functional comparisons of the eukaryotic and prokaryotic isoforms". Biochimie. 77 (7-8): 562–72. doi:10.1016/0300-9084(96)88172-7. PMID 8589067. 
  • Wang M, Roberts DL, Paschke R, Shea TM, Masters BS, Kim JJ (1997). "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes". Proc. Natl. Acad. Sci. U.S.A. 94 (16): 8411–6. doi:10.1073/pnas.94.16.8411. PMC 22938Freely accessible. PMID 9237990. 
  • Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK (2001). "Determination of the redox properties of human NADPH-cytochrome P450 reductase". Biochemistry. 40 (7): 1956–63. doi:10.1021/bi001718u. PMID 11329262. 
  • Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK (2001). "Determination of the redox properties of human NADPH-cytochrome P450 reductase". Biochemistry. 40 (7): 1956–63. doi:10.1021/bi001718u. PMID 11329262. 
  • Scrutton NS; Grunau, A; Paine, M; Munro, AW; Wolf, CR; Roberts, GC; Scrutton, NS (2003). "Electron transfer in human cytochrome P450 reductase". Biochem. Soc. Trans. 31 (Pt 3): 497–501. doi:10.1042/BST0310497. PMID 12773143. 
  • Scrutton NS; Grunau, A; Paine, M; Munro, AW; Wolf, CR; Roberts, GC; Scrutton, NS (2003). "Electron transfer in human cytochrome P450 reductase". Biochem. Soc. Trans. 31 (Pt 3): 497–501. doi:10.1042/BST0310497. PMID 12773143.