Titlebook: Cytochrome P450; Structure, Mechanism Paul R. Ortiz Montellano Book 1995Latest edition Springer-Verlag US 1995 NADPH.Oxidation.biochemistry

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S. Blot,D. Koulenti,G. Dimopoulos. Cytochrome P450 is known to catalyze hydroxylations, epoxidations, .-, .-, and .-dealkylations, .-oxidations, sulfoxidations, dehalogenations, and other reactions.. The reactive site of all of these enzymes is extraordinarily simple, containing only an iron protoporphyrin IX (.) (Fig. 1) with cyst

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M. Carlier,V. Stove,J. J. De Waele between peroxidases and P450s include the ability of P450s to accept electrons from a reductase; the redox potentials of the higher oxidation states; and the ability of P450s to generate the equivalent of a metal-bound peroxide by reduction of O. at the heme center during catalytic turnover.

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P. M. Honoré,R. Jacobs,H.D. Spapen is well documented.) Thus, scientists have become interested in the mechanisms of disease states resulting from mutations in P450s, and in alternative substrates metabolized and new products formed by the engineering of known P450 proteins. Only through an understanding of the structures of these p

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C. Chiurazzi,A. Motos-Galera,A. Torresnd transfer of electrons from the flavin centers to oxygen and/or the redox partners of cytochrome P450 reductase. This present review, therefore, will not cover mechanism in any more than a cursory fashion, but will attempt to focus on a summary of the salient features of the study of structural/fu

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Light and Shade of New Antibioticsetoxification, particularly when low to moderate concentrations of substrate are present; thus, under most conditions, induction is a protective mechanism, whereby the cell can detoxify lipophilic compounds that might otherwise accumulate. Both characteristics are likely to facilitate the survival o

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M. Chan,M. Varrier,M. Ostermannenation reactions, and (3) the decoding of that chemical information either by receptor-mediated processes or, alternatively, by the direct effects of these oxygenated metabolites on metabolic pathways. (Fig. 1). As a net result, these processes provide cells with a rapid and versatile on/off molecu

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J. Izawa,A. Zarbock,J. A. Kellumme-thiolate proteins, the cytochromes P450 responsible for monooxygenation reactions (which will be called “classical P450s” in this chapter) have been extensively studied. and their mechanisms of dioxygen activation and substrate hydroxylation are now well established.. During these last years, som