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Substrate binding induces structural changes in cytochrome P450cam.

Keisuke Sakurai1, Hideo Shimada, Takashi Hayashi

  • 1Institute for Protein Research, Osaka University, Suita 565-0871, Japan.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
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PubMed
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Camphor binding to cytochrome P450cam expels water, increasing its redox potential. This occurs via a specific protein structural change involving Thr101 rotation and hydrogen bond formation.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Enzymology

Background:

  • Cytochrome P450cam (P450cam) is a key enzyme involved in substrate metabolism.
  • Substrate binding to P450cam is known to alter its redox potential, facilitating electron transfer.
  • Previous studies suggested minimal protein structural changes upon camphor binding.

Purpose of the Study:

  • To elucidate the structural basis of (+)-camphor binding to P450cam.
  • To investigate the mechanism by which substrate binding affects the enzyme's redox potential.
  • To resolve the structures of both substrate-free and substrate-bound P450cam.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structures (1.30-1.35 Å) of ferric P450cam.
  • Structures of both partially substrate-complexed and substrate-free forms were resolved.

Main Results:

  • The binding of (+)-camphor induces a specific structural rearrangement in P450cam.
  • Threonine 101 (Thr101) rotates to form a novel hydrogen bond.
  • This hydrogen bond acts as a hydrogen donor to a peripheral heme propionate, contributing to the observed redox potential shift.

Conclusions:

  • The structural data reveal a specific mechanism for redox potential modulation in P450cam upon substrate binding.
  • The rotation of Thr101 and subsequent hydrogen bond formation are critical for facilitating electron transfer.
  • This finding provides a detailed molecular understanding of enzyme-substrate interactions and their functional consequences.