Cytochromes P450: Structure, Function and Mechanism (Taylor - download pdf or read online

By David F.V. Lewis

ISBN-10: 0748404430

ISBN-13: 9780748404438

This consultant to the constitution, functionality and mechanism of the cytochromes P450 makes a speciality of the position of P450s in xenobiotic metabolism and toxicity. color illustrations convey how modelling of P450s can rationalize their substrate specificity for the metabolism of either endogenous and exogenous chemical substances.

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Extra info for Cytochromes P450: Structure, Function and Mechanism (Taylor & Francis Series in Pharmaceutical Sciences)

Example text

In fact, the ESR spectra of P450s show that they represent a distinct class of hemoprotein in terms of the geometry of the heme iron, as affected by the nature of the apoprotein and its conformation (Blumberg and Peisach, 1971). However, considerable information has also been accumulated from optical spectroscopic techniques, mainly using UV absorption spectrophotometry. In terms of ligand characteristics, the thiolate ion is an extremely weak ligand and a ‘soft’ base, which is also a -donor; whereas, in contrast, water is a medium strength ligand and a ‘hard’ base, and carbon monoxide is a very strong ligand and -acceptor, as is oxygen although slightly less strong than CO (da Silva and Williams, 1991).

Unfortunately, ferroheme will also have a high affinity for the highly toxic gas carbon monoxide, as well as for the cyanide ion, which are both good INTRODUCTION 11 -acceptor ligands. 22 Å. CO-P450 complex were instrumental both in the discovery of the enzyme and its name, which derives from the UV absorption maximum of the CO-complex (Sato and Omura, 1978). The axial heme ligands impart a number of properties to the hemoprotein which dictates its biological role, in addition to the means of detection by spectroscopic and other physical techniques.

1991). 5) to the vibrational stretching frequency, this suggests that activation of dioxygen by P450 decreases the O−O bond energy and increases the bond length, such that bond cleavage will occur, thus leading to monoxygenation of the substrate. , 1992). , 1992). 15). 39 Å between the two oxygens (Lewis and Lake, 1995) is too long for any hydrogen bond formation. However, the possibility of free rotation of the T252 side chain can shorten this distance by almost 1Å and, in the case of the dioxygen complex, the longer O−O bond makes ligand-protein hydrogen-bonding fairly likely.

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Cytochromes P450: Structure, Function and Mechanism (Taylor & Francis Series in Pharmaceutical Sciences) by David F.V. Lewis

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