Flavin enzymes: molecular orbital calculations
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Updated: Jun 28, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
W R Carper1, M Q Freeland, F R Duke
1Department of Chemistry, Texas A&M University, College Station, Texas, U.S.A.
Abstract:
Molecular orbital calculations were obtained for one hundred and forty-four versions of the flavin group contained in oxidase enzymes. Ten different structures were considered and the results indicate that the flavin group changes its identity from a pi electron acceptor to a pi electron donor after reduction occurs, regardless of the inductive effect of the attached protein. Furthermore, the calculations suggest both the site for reduction and the mechanism by which it proceeds.
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