NADPH—hemoprotein reductase

NADPH—hemoprotein reductase
NADPH-Cytochrome P450 reductase dimer, Rattus norvegicus
Identifiers
EC no.	1.6.2.4
CAS no.	9023-03-4
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

NADPH + H⁺ + n oxidized hemoprotein $\rightleftharpoons$ NADP⁺ + n reduced hemoprotein

The three substrates of this enzyme are NADPH, H⁺, and oxidized hemoprotein, whereas its two products are NADP⁺ and reduced hemoprotein. It has two cofactors: flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN).

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 include cytochrome P450 reductase, ferrihemoprotein P-450 reductase, and NADPH-dependent cytochrome c reductase.

Structural studies

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

References

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• 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. Bibcode:1997PNAS...94.8411W. doi:10.1073/pnas.94.16.8411. PMC 22938. 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. hdl:2381/11955. 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. hdl:2381/11955. PMID 12773143.