Allosteric Transitions in Cytochrome P450eryF Explored with Pressure-Perturbation Spectroscopy, Lifetime FRET, and a Novel Fluorescent Substrate, Fluorol-7GA-Reference-Cited by-同舟云学术

Allosteric Transitions in Cytochrome P450eryF Explored with Pressure-Perturbation Spectroscopy, Lifetime FRET, and a Novel Fluorescent Substrate, Fluorol-7GA

Published:2008-10-02 Issue:43 Volume:47 Page:11348-11359
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Davydov Dmitri R.¹,Davydova Nadezhda Y.¹,Halpert James R.¹

Affiliation:

1. Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093-0703

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8011803

Reference50 articles.

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2. Analysis of human cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics

3. Evaluation of Atypical Cytochrome P450 Kinetics with Two-Substrate Models: Evidence That Multiple Substrates Can Simultaneously Bind to Cytochrome P450 Active Sites

4. Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity

5. Resolution of Two Substrate-Binding Sites in an Engineered Cytochrome P450eryF Bearing a Fluorescent Probe

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