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A functional proline switch in cytochrome P450cam.

Bo OuYang1, Susan Sondej Pochapsky, Marina Dang

  • 1Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02454-9110, USA.

Structure (London, England : 1993)
|June 3, 2008
PubMed
Summary
This summary is machine-generated.

Putidaredoxin (Pdx) binding induces a conformational change in cytochrome P450(cam) (CYP101), enabling efficient camphor hydroxylation. This involves an X-proline bond isomerization, crucial for enzyme function and Pdx binding.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • The putidaredoxin-cytochrome P450(cam) (Pdx-CYP101) complex is essential for camphor hydroxylation.
  • Understanding the structural dynamics of CYP101 upon Pdx binding is key to elucidating its catalytic mechanism.

Purpose of the Study:

  • To investigate the conformational changes in CYP101 induced by Pdx binding.
  • To determine the role of X-proline isomerization in the Pdx-CYP101 interaction and catalytic activity.

Main Methods:

  • Site-directed mutagenesis of CYP101, specifically at proline 89 and isoleucine 88.
  • Analysis of camphor binding orientations using experimental evidence.
  • Assessing the impact of mutations on Pdx binding affinity.

Main Results:

  • Pdx binding induces a conformational shift in CYP101, reorienting bound camphor for optimal hydroxylation.
  • Pdx binding triggers the isomerization of a specific X-proline amide bond in CYP101 from trans to cis.
  • Mutations affecting the cis conformer of the Ile88-Pro89 amide bond weaken Pdx binding.

Conclusions:

  • X-proline isomerization is a critical event in the Pdx-CYP101 complex formation and function.
  • Conformational changes driven by isomerization are essential for efficient enzymatic catalysis in CYP101.
  • This study provides direct evidence for the involvement of X-proline isomerization in enzyme mechanisms.