Abstract
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. © 2013 American Chemical Society.
Recommended Citation
R. Robinson et al., "C4a-hydroperoxyflavin Formation in N -hydroxylating Flavin Monooxygenases is Mediated by the 2′-OH of the Nicotinamide Ribose of NADP⁺," Biochemistry, vol. 52, no. 51, pp. 9089 - 9091, American Chemical Society, Dec 2013.
The definitive version is available at https://doi.org/10.1021/bi4014903
Department(s)
Chemistry
International Standard Serial Number (ISSN)
1520-4995; 0006-2960
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 American Chemical Society, All rights reserved.
Publication Date
23 Dec 2013
PubMed ID
24321106
Comments
National Science Foundation, Grant 1021384