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Substrate binding favors enhanced NO binding to P450cam.

Alicja Franke1, Grazyna Stochel, Christiane Jung

  • 1Institute for Inorganic Chemistry, University of Erlangen-Nürnberg, Egerlandstr. 1, 91058 Erlangen, Germany.

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Summary

Cytochrome P450cam binds nitric oxide (NO), with substrate camphor significantly altering binding kinetics. This study clarifies NO binding mechanisms in P450cam using pressure and spectroscopy.

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Area of Science:

  • Biochemistry
  • Chemical Kinetics
  • Spectroscopy

Background:

  • Cytochrome P450cam (P450cam) is a key enzyme involved in various biological processes.
  • Nitric oxide (NO) is an important signaling molecule that interacts with heme proteins.

Purpose of the Study:

  • To investigate the effect of substrate (1R-camphor) on the binding kinetics of NO to ferric P450cam.
  • To elucidate the reaction mechanisms of NO binding and release using high-pressure techniques.

Main Methods:

  • Laser flash photolysis
  • Stopped-flow spectroscopy
  • High-pressure studies

Main Results:

  • Substrate presence significantly enhances NO association and dissociation rates.
  • Substrate-free P450cam exhibits slow NO binding kinetics with positive activation entropy and volume.
  • Camphor-bound P450cam shows fast NO binding with negative activation entropy and volume, indicating a bond formation-dominated mechanism.

Conclusions:

  • The substrate dramatically influences the NO binding mechanism of P450cam, shifting from a dissociative to an associative process.
  • Volume profiles provide insights into the molecular-level mechanisms of NO interaction with heme proteins.
  • Understanding these mechanisms is crucial for the biological function of cytochrome P450 enzymes.