The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference35 articles.
1. Transformation of cholesterol and acetate to adrenal cortical hormones
2. Partial resolution of the mixed-function oxidase involved in the cholesterol side-chain cleavage reaction in bovine adrenal mitochondria
3. Adrenal cortex mitochondrial cytochrome P-450 specific to cholesterol side chain cleavage reaction. Spectral changes induced by detergents, alcohols, amines, phospholipids, steroid hydroxylase inhibitors, and steroid substrates, and conditions for adrenodoxin binding to the cytochrome.
4. Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle.
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1. Effect of steroid biosynthesis modifiers on progesterone biotransformation by recombinant yeasts expressing cytochrome P450cl7;Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry;2007-03
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3. Coexpression of all constituents of the cholesterol hydroxylase/lyase system in Escherichia coli cells;Biochemistry (Moscow);2006-07
4. Light-Induced Reduction of Bovine Adrenodoxin via the Covalently Bound Ruthenium(II) Bipyridyl Complex: Intramolecular Electron Transfer and Crystal Structure;Biochemistry;2005-12-22
5. Formation and Functioning of Fused Cholesterol Side-Chain Cleavage Enzymes;DNA and Cell Biology;2003-04
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