Journal
BIOCHEMISTRY
Volume 52, Issue 51, Pages 9089-9091Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi4014903
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- National Science Foundation [MCB-1021384]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1021384] Funding Source: National Science Foundation
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Flavin-dependent monooxygenases must stabilize a C4a-hydroperoxyflavin intermediate to hydroxylate their respective substrates. Formation and decay of the C4a-hydroperoxyflavin were monitored under rapid reaction kinetic conditions in SidA, an N-hydroxylating monooxygenase involved in siderophore biosynthesis. Solvent kinetic isotope effect studies of flavin oxidation indicate that both hydrogen peroxide elimination and water elimination occur via abstraction of hydrogen from the N5 of the flavin. Kinetic isotope effect and density functional theory results are consistent with the transfer of a proton from the 2'-OH of the nicotinamide ribose of nicotinamide adenine dinucleotide phosphate (NADP(+)) to the C4a-peroxyflavin to form the C4a-hydroperoxyflavin. This represents a novel role for NADP(+) in the reaction of flavin-dependent enzymes.
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