Cytochrome P-450: Structure, Mechanism, and Biochemistry by Thomas J. McMurry, John T. Groves (auth.), Paul R. Ortiz de

By Thomas J. McMurry, John T. Groves (auth.), Paul R. Ortiz de Montellano (eds.)

Major advances were made lately in clarifying the molecular homes of the cytochrome P-450 method. those advances stem, in sensible phrases, from the widely famous value of cytochrome P-450 within the metabolism of substances and within the bioactivation of xenobiotics to poisonous items. The attention-grabbing multiplicity and differential rules of cytochrome P-450 isozymes, and their skill to catalyze terribly tricky chemical modifications, have independently drawn many chemists and biochemists into the P-450 circle. growth within the box, from a technical standpoint, has been propelled via the de­ velopment of trustworthy approaches for the purification of membrane-bound enzymes, by way of the transforming into repertoire of molecular organic thoughts, and by means of the advance of chemical types that mimic the catalytic motion of P-450. therefore, our realizing of the P-450 method is relocating from the descriptive, pharmacological point into the tangible realm of atomic element. The swift growth and multidisciplinary personality of the cytochrome P-450 box, which cuts around the traces that typically divide disciplines as various as inorganic chemistry and genetics, have created a necessity for an up to date assessment of the advances which have been made. it's was hoping that this booklet, with its molecular specialize in the cytochrome P-450 process, will alleviate this desire. The authors of the person chapters have strived to stress fresh effects with no sacrificing the history required to make their chapters understandable to knowledgeable nonspecialists.

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Extra info for Cytochrome P-450: Structure, Mechanism, and Biochemistry

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And Bierbaum, V. , 1984, Oxidation of alkenes by d0 transition-metal oxo species: A mechanism for the oxidation of ethylene by a dioxochromium(Vl) complex in the gas phase, Organometallics 3:498-499. , 1983, Monooxygenase-like dioxygen activation leading to alkane hydroxylation and olefin epoxidation by an Mnm (porphyrin)-ascorbate biphasic system, J. Chern. Soc. Chern. Commun. 1983:253-254. , 1979, P-450 type oxygen activation by porphyrin-man- 28 CHAPTER 1 ganese complex, J. Am. Chern. Soc.

57 The latter observation suggests that the organic functionality of the hydroperoxide is present in the oxidizing agent that plays a role in hydroxylation. None of these findings are consistent with the paradigm for oxidations catalyzed by peroxidases. Rather, they suggest that P-450 reduces hydroperoxides by one electron to form an alkoxyl radical and a ferryl-hydroxo complex, both CHAPTER 2 42 N 100 o;-E 80 u ~80 20 0 ~--~L---~----~----~ 380 400 420 440 460 380 400 420 440 480 WAVELENGTH (nm) FIGURE 6.

The mechanism of 0-0 bond scission and, in particular, the chemistry of hydroperoxy iron porphyrins have not been extensively explored. 22 CHAPTER 1 These and related issues form the current focus of the chemistry of P450. References I. Hayaishi, 0. ), 1974, The Molecular Mechanisms qfOxygen Activation, Academic Press, New York. 2. Groves, J. , 1979, Cytochrome P-450 and other hemecontaining oxygenases, Adv. Inorg. Biochem. 1:119-145. 3. (a) White, R. , and Coon, M. , 1980, Oxygen activation by cytochrome P-450, Annu.

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