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  3. Hole Migration In Cytochrome P450.
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Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
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Published on: June 1, 2022

Hole migration in cytochrome P450.

Harry Gray1, Jay Winkler2

  • 1California Institute of Technology Chemistry & Chemical Engineering Faculty, USA.

QRB Discovery
|May 14, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

Cytochrome P450 enzymes use compound I (CI) for hydroxylation. Kinetics simulations show CI hole lifetimes on hemes range from ~100 ns to ~100 μs, impacting enzyme efficiency and protection.

Keywords:
CYP102A1CYP119CYP158A2CYP3A4electron transfer

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Area of Science:

  • Biochemistry
  • Enzymology
  • Chemical Kinetics

Background:

  • Cytochrome P450 enzymes are crucial for metabolizing organic compounds via dioxygen-dependent hydroxylation.
  • The catalytic cycle involves a high-potential reactive intermediate, compound I (CI), capable of oxidizing amino acid residues.

Purpose of the Study:

  • To model the kinetics of hole transfer from the heme to redox-active amino acid residues (tryptophan, tyrosine, cysteine) in P450 enzymes.
  • To understand the factors influencing the survival lifetime of the reactive intermediate and its implications for enzyme function.

Main Methods:

  • Utilized X-ray crystal structure coordinates of four P450 enzymes.
  • Applied semiclassical theory of electron transfer to model hole transfer kinetics.
  • Employed Monte Carlo sampling to address uncertainties in redox potentials.

Main Results:

  • Simulated mean hole survival lifetimes on heme groups ranged from approximately 100 nanoseconds to 100 microseconds.
  • Identified that hole transfer to enzyme surface residues can decrease substrate oxidation efficiency.

Conclusions:

  • Hole transfer kinetics play a significant role in P450 enzyme efficiency and stability.
  • While potentially reducing catalytic efficiency, surface hole transfer may serve a protective role against enzyme damage when substrate binding or reaction fails.