An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals

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Abstract

The recent determination of the amino acid sequences of theBacillus megaterium cytochrome P-450 and the flavoprotein component ofSalmonella 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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