Isotope-Labeling Studies Support the Electrophilic Compound I Iron Active Species, FeO3+, for the Carbon–Carbon Bond Cleavage Reaction of the Cholesterol Side-Chain Cleavage Enzyme, Cytochrome P450 11A1
Author:
Affiliation:
1. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, United States
Funder
National Cancer Institute
Vanderbilt University School of Medicine
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.6b04437
Reference55 articles.
1. Pregnenolone formation from cholesterol in bovine adrenal cortex mitochondria: Proposal of a new mechanism
2. Sterol metabolism VIII. Conversion of cholesterol 20α-hydroperoxide to 20α, 21- and 20α,22R-dihydroxycholesterol by adrenal cortex mitochondria
3. Enzymatic formation of (20R,22R)-20,22-dihydroxycholesterol from cholesterol and a mixture of 16O2 and 18O2: Random incorporation of oxygen atoms
4. Compound I Is the Reactive Intermediate in the First Monooxygenation Step during Conversion of Cholesterol to Pregnenolone by Cytochrome P450scc: EPR/ENDOR/Cryoreduction/Annealing Studies
5. Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing Studies
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