Cytochrome P450 enzymes catalyze a variety of reactions, such as detoxication of drugs and carcinogens, biosynthesis of steroid hormones, vitamin activation, etc. Electrons, required for oxidation of substrates, are being delivered to P450s by either iron-sulfur proteins or FAD/FMN-containing NADPH-cytochrome P450 reductase. How P450s interact with their redox partners and what is the mechanism of electron transfer are the key questions in mechanism and function of P450 enzymes. Cytochrome P450BM-3, a soluble fusion protein consisting of both the heme- and reductase domains on a single polypeptide chain, is the best model for studying P450-P450 reductase interactions. We crystallized a 75 kDa fragment of this enzyme, consisting of both the heme- and FMN-binding domains. Large unit cell and poor diffraction pattern, obtained using in-house X-ray source, do not allow us to refine this structure.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6119473
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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