What question did this study set out to answer?

The research investigates the kinetics and mechanisms of hole migration in cytochrome P450 enzymes during substrate hydroxylation.

May 6, 2026QRB DiscoveryOpen Access

Hole migration in cytochrome P450

View Full Paper

Ask AI

Bookmark

Authors

Modeling kinetics of hydroxylation in cytochrome P450 reveals that hole transfer to tryptophan impacts oxidation efficiency.

The research investigates the kinetics and mechanisms of hole migration in cytochrome P450 enzymes during substrate hydroxylation.
Utilized X-ray crystal structure coordinates for modeling P450 enzyme kinetics.
Applied semiclassical theory of electron transfer for hole transfer simulations.
Performed Monte Carlo sampling to assess reaction driving forces and uncertainties.
Identified the reactive intermediate compound I's role in delivering oxidizing equivalents.
Determined mean survival lifetimes of holes on the hemes range from ~100 ns to ~100 μs.
Showed that hole transfer to redox-active residues can reduce substrate oxidation efficiency but provide protection to the enzyme.

Gray et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark