NADPH—hemoprotein reductase

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, , , , , , , , , and.