Biology:NADPH—hemoprotein reductase

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Short description: Enzyme

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

NADPH + H+ + n oxidized hemoprotein [math]\displaystyle{ \rightleftharpoons }[/math] 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. It has 2 cofactors: FAD, and 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.

References