Published September 4, 2002
| Supplemental Material
Journal Article
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Fluorescent Probes for Cytochrome P450 Structural Characterization and Inhibitor Screening
Chicago
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Abstract
We have synthesized two luminescent probes (D-4-Ad and D-8-Ad) that target cytochrome P450cam. D-4-Ad luminescence is quenched by Förster energy transfer upon binding (K_d = 0.83 μM) but is restored when the probe is displaced from the active site by camphor. In contrast, D-8-Ad (K_d ≈ 0.02 μM) is not displaced from the enzyme, even in the presence of a large excess of camphor. The 2.2 Å resolution crystal structure of the D-8-Ad:P450cam complex reveals extensive hydrophobic contacts between the probe and the enzyme, which result from the conformational flexibility of the B', F, and G helices. Probes with properties similar to those of D-4-Ad potentially could be useful for screening P450 inhibitors.
Additional Information
© 2002 American Chemical Society. Received June 4, 2002. Publication Date (Web): August 10, 2002. This work was supported by the Fannie and John Hertz Foundation (A.R.D.), the National Science Foundation, and the National Institutes of Health (Metalloprotein Program Project Grant P01 GM48495; NRSA fellowship GM20703 to A.-M.A.H.).Attached Files
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Additional details
- Eprint ID
- 76801
- Resolver ID
- CaltechAUTHORS:20170421-083018566
- Fannie and John Hertz Foundation
- NSF
- NIH
- P01 GM48495
- NIH Predoctoral Fellowship
- GM20703-03
- Created
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2017-04-21Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field