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Publication Detail

Title: Mechanism of cytochrome P450 reductase from the house fly: evidence for an FMN semiquinone as electron donor.

Authors: Murataliev, M B; Feyereisen, R

Published In FEBS Lett, (1999 Jun 18)

Abstract: The interaction of recombinant house fly (Musca domestica) P450 reductase with NADPH and the role of the FMN semiquinone in reducing cytochrome c have been investigated. House fly P450 reductase can rapidly oxidize only one molecule of NADPH, whereas the rate of oxidation of a second molecule of NADPH is too slow to account for the observed rates of catalysis. This demonstrates that house fly P450 reductase does not require a priming reaction with NADPH for catalysis. Kinetics of cytochrome c reduction and EPR spectroscopy revealed that the enzyme forms two types of neutral FMN semiquinone. One serves as the catalytic intermediate of cytochrome c reduction, and another one is an 'airstable' semiquinone, which reduces cytochrome c 3000 times more slowly. The results show that the reduction state of the house fly P450 reductase during catalysis cycles in a 0-2-1-0 sequence.

PubMed ID: 10403403 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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