Substrate binding induces structural changes in cytochrome P450cam
2009
Structural Changes in Cytochrome P450cam Induced by Substrate Binding
publication
Evidence: high
Author Information
Author(s): Sakurai Keisuke, Shimada Hideo, Hayashi Takashi, Tsukihara Tomitake
Primary Institution: Institute for Protein Research, Osaka University
Hypothesis
How does the binding of (+)-camphor affect the structure and redox potential of cytochrome P450cam?
Conclusion
The binding of (+)-camphor induces structural changes in cytochrome P450cam that raise the redox potential of the haem iron.
Supporting Evidence
- The binding of (+)-camphor expels a cluster of water molecules at the active site.
- Thr101 forms a hydrogen bond with the haem 6-propionate upon substrate binding.
- The redox potential of the haem iron is raised by approximately 100 mV due to substrate binding.
Takeaway
When a substance called (+)-camphor sticks to a protein called cytochrome P450cam, it changes the protein's shape and helps it work better.
Methodology
X-ray crystallography was used to determine the structures of substrate-free and substrate-bound forms of cytochrome P450cam.
Digital Object Identifier (DOI)
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