NADPH—hemoprotein reductase

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

NADPH + H⁺ + n oxidized hemoprotein ${\displaystyle \rightleftharpoons }$ NADP⁺ + n reduced hemoprotein

NADPH—hemoprotein reductase
NADPH-Cytochrome P450 reductase dimer, Rattus norvegicus
Identifiers
EC no.	1.6.2.4
CAS no.	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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 1AMO, 1B1C, 1J9Z, 1JA0, 1JA1, 1YQO, 1YQP, 2BF4, 2BN4, and 2BPO.