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Updated: Aug 14, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals
1Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor 48109-0606.
Abstract:
The recent determination of the amino acid sequences of the Bacillus megaterium cytochrome P-450 and the flavoprotein component of Salmonella typhimurium NADPH-sulfite reductase revealed that these enzymes contain a flavoprotein moiety remarkably similar to mammalian NADPH-cytochrome P-450 reductase. The presence of this oxidoreductase in these very different enzymes suggests that this flavoprotein arose early in evolution and was utilized as an enzymological building block. The multi-domain structure of the reductase further suggests that it arose through a fusion of genes encoding simple flavin electron-transport proteins.
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