Interplay between two spin states determines the hydroxylation catalyzed by P450 monooxygenase from Trichoderma brevicompactum
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Updated: Dec 28, 2025

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Razak Hussain1, Rolly Yadav2, Mushtaq Ahmed3
1Department of Botany, Aligarh Muslim University, Aligarh, Uttar Pradesh, India.
Abstract:
Tri11 (now renamed as tri22) encoded cytochrome P450 monooxygenase in Trichoderma brevicompactum catalyzes the C-4 C-H hydroxylation of 12, 13-epoxytrichothec-9-ene (EPT) to produce trichodermol in the biosynthetic pathway of trichodermin/harzianum A. The density functional theory (DFT)-quantum mechanics (QM) approach is applied to elucidate the hydroxylation of EPT by using a model active species of P450 (Cpd I). The QM calculations were performed on the active site complex, to find out transition-state structure, intermediate, and product complexes for the two spin states at different potential energy surfaces. The two state reactivity rebound-free product formation resulted from the interplay of two spin states (doublet and quartet).
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