Studies of the unique nature of the cytochrome P-450 active site. Electron spin resonance spectroscopy as a probe of the hemin iron of cytochrome P-450: the influence of buffer composition, alcohols, and nitrogenous ligands.
D000476:Alkanesulfonates; D000818:Animals; D001665:Binding Sites; D002021:Buffers; D002164:Camphor / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000031:analogs & derivatives; D006427:Hemin; D008297:Male; D008566:Membranes; D000432:Methanol; D008748:Methylcholanthrene / Q000494:pharmacology; D008797:Metyrapone; D008862:Microsomes, Liver; D009025:Morpholines; D010634:Phenobarbital / Q000494:pharmacology; D011549:Pseudomonas; D051381:Rats
D000476:Alkanesulfonates; D002021:Buffers; D009025:Morpholines; D006418:Heme; D008748:Methylcholanthrene; D006427:Hemin; D002164:Camphor; D003577:Cytochrome P-450 Enzyme System; D000432:Methanol; D010634:Phenobarbital; D008797:Metyrapone