The presence of an adrenodoxin-like ferredoxin and cytochrome P-450 in brain mitochondria.
An iron-sulfur protein has been isolated from bovine brain mitochondria and purified 200-fold. The optical spectrum (peaks at 412 and 455 nm which disappear upon reduction) and the EPR spectrum (g values at 1.94 and 2.02) were typical for a ferredoxin. In reconstitution experiments, the protein could replace adrenodoxin in the cholesterol side chain cleavage reaction. The additional detection of cytochrome P-450 in brain mitochondria indicates that the isolated ferredoxin is part of a cytochrome P-450-dependent hydroxylation system.
D000325:Adrenodoxin / Q000032:analysis* / Q000302:isolation & purification; D000818:Animals; D001921:Brain / Q000378:metabolism; D001923:Brain Chemistry; D002248:Carbon Monoxide; D002417:Cattle; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D005288:Ferredoxins / Q000032:analysis* / Q000302:isolation & purification; D008928:Mitochondria / Q000032:analysis*; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D013347:Subcellular Fractions / Q000032:analysis
D005288:Ferredoxins; D000325:Adrenodoxin; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System