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Updated: Feb 5, 2026
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Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c
Published on: June 29, 2011
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Substrate-induced conformational change in cytochrome P450 OleP
Giacomo Parisi1,2, Linda Celeste Montemiglio1,2,3, Alessandro Giuffrè3
1Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Sapienza Università di Roma, Rome, Italy.
Summary
Cytochrome P450 OleP undergoes significant structural changes upon substrate binding, revealing a complex mechanism involving intermediate states. These findings illuminate how substrate-induced conformational transitions regulate enzyme activity.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Cytochrome P450 enzymes are crucial in biosynthesis and drug metabolism.
- Enzyme activity is often regulated by conformational changes induced by substrate binding.
Purpose of the Study:
- To elucidate the substrate-induced conformational transition in P450 OleP, an epoxygenase.
- To provide structural insights into the precatalytic steps of OleP activity.
Main Methods:
- X-ray crystallography of OleP bound to a substrate analog (6DEB).
- Kinetic analysis of OleP-6DEB binding, including inhibition studies with clotrimazole.
- Spectroscopic characterization of reaction intermediates.
Main Results:
- Crystallization of OleP-6DEB revealed both open and closed conformations.
- A complex binding mechanism was identified, featuring slow conformational rearrangement.
- A spectroscopically detectable intermediate with substrate bound to open OleP was observed.
Conclusions:
- Substrate binding induces significant conformational changes in P450 OleP.
- These structural rearrangements are key to regulating OleP's catalytic activity.
- The study provides structural snapshots of critical precatalytic steps in the OleP reaction.
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