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

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Inhibition of Cytochrome P450 Enzymes substrates, (2) the binding of molecular oxygen subsequent to the first electron transfer, and (3) the catalytic step in which the substrate is actually oxidized. This chapter focuses on inhibitors that act at one of these three steps. Inhibitors that act at other steps in the catalytic cycle, such

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Hormonal Regulation of Liver Cytochrome P450 Enzymes and other tissues,. including the primary steroidogenic tissues (Kagawa and Waterman, this volume). Steroid hormones are metabolized by liver P450 enzymes with a higher degree of regio-and stereoselectivity than many foreign compound substrates,. suggesting that these endogenous lipophiles serve as

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Regulation of Steroidogenic and Related P450sogenous substrates (xenobiotics). Those forms that metabolize endogenous substrates generally convert less active compounds into more active ones. This is particularly true of the P450s that participate in steroid hormone biosynthesis, where the less active steroid cholesterol is converted into more

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Heme-Thiolate Proteins Different from Cytochromes P450 Catalyzing Monooxygenationse been found in living organisms.. On the contrary, only a limited number of hemoprotein families where the heme iron is bound to a cysteinate proximal ligand have been discovered so far. The Fe(II)-CO complex of these hemoproteins is most often characterized by a visible spectrum exhibiting a redsh

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Structures of Eukaryotic Cytochrome P450 Enzymesferent eukaryotic members of the cytochrome P450 superfamily. Such information would provide insights into the structural arrangement of these proteins that would assist in the rational design of therapeutic enzyme inhibitors or in the engineering of P450s as biotechnological tools.

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