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Carla E. Meints, Svetlana Simtchouk and Kirsten R. Wolthers Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase The FEBS Journal 280

Version of Record online: 15 FEB 2013 | DOI: 10.1111/febs.12141

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Substitution of a conserved FAD-shielding tryptophan with Phe or Tyr, increased catalysis in methionine synthase reductase (MSR) and diminished the rate of flavin reduction in cytochrome P450 reductase (CPR). Our results suggest that movement of Trp away from the FAD “gates” NADPH hydride transfer in MSR, while in CPR, the corresponding Trp lowers the energy barrier for displacement of NADP+.

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