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EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
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Conformational selectivity in cytochrome P450 redox partner interactions.

Scott A Hollingsworth1, Dipanwita Batabyal1, Brian D Nguyen1

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697; Department of Pharmaceutical Sciences, University of California, Irvine, CA 92697; Department of Chemistry, University of California, Irvine, CA 92697.

Proceedings of the National Academy of Sciences of the United States of America
|July 22, 2016
PubMed
Summary

Cytochromes P450 require reduction by redox partners for activity. This study confirms that putidaredoxin (Pdx) binding favors the open conformation of P450cam, crucial for oxygen activation and catalysis.

Keywords:
P450conformationredox partner

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Cytochromes P450 (P450s) catalyze crucial oxidative reactions, requiring heme iron reduction.
  • Redox partners form protein-protein complexes with P450s to deliver electrons.
  • The role of redox partner binding in inducing conformational changes in P450s for activity is debated.

Purpose of the Study:

  • To resolve conflicting data on whether putidaredoxin (Pdx) binding favors an open or closed conformation of P450cam.
  • To clarify the structural implications of Pdx binding on P450cam activity.

Main Methods:

  • Computational analysis of molecular dynamics trajectories.
  • Experimental isothermal titration calorimetry (ITC) studies.
  • Structural and spectral analyses of P450cam.

Main Results:

  • Putidaredoxin (Pdx) unequivocally favors binding to the open conformation of P450cam.
  • Molecular dynamics simulations provided insights into intermediate conformational states.
  • ITC data confirmed the preference for Pdx binding to the open P450cam form.

Conclusions:

  • Pdx binding stabilizes the open conformation of P450cam, which is necessary for substrate oxidation.
  • Understanding these conformational dynamics is vital for P450-mediated catalysis.
  • This work reconciles discrepancies regarding P450cam-Pdx interactions.