Steroid binding properties of beef adrenal cortical cytochrome P-450 which catalyzes the conversion of cholesterol into pregnenolone.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Separation of two forms of cytochromeP450 adrenal cortex mitochondria
2. Cytochrome P-450 from Bovine Adrenocortical Mitochondria: an Enzyme for the Side Chain Cleavage of Cholesterol
3. Purification and characterization of adrenal cortex mitochondrial cytochrome P-450 specific for cholesterol side chain cleavage activity.
4. Purification of cytochrome P-450 from bovine adrenocortical mitochondria by an “Aniline-sepharose” and the properties
5. Substrate induced spin state changes in cytochrome P450
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2. 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;Biochemistry;2015-11-25
3. 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;Journal of the American Chemical Society;2012-10-05
4. Features of the retinal environment which affect the activities and product profile of cholesterol-metabolizing cytochromes P450 CYP27A1 and CYP11A1;Archives of Biochemistry and Biophysics;2012-02
5. Structural Basis for Three-step Sequential Catalysis by the Cholesterol Side Chain Cleavage Enzyme CYP11A1;Journal of Biological Chemistry;2011-02
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