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

By David F.V. Lewis

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

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

Sample text

In fact, in terms of per cent rhombicity P450s resemble some of the modified hemoglobins and myoglobins, with one of the mutant human hemoglobins, namely hemoglobin MHyde Park, lying within the same characteristic region of rhombicity and tetragonal field as the P450s (Blumberg and Peisach, 1971). e. the mutation is of the form H92Y) and, presumably, this produces some similarity in the heme geometry and electronic state to that caused by cysteine ligation in P450, by pushing electron density towards the heme.

1981). , 1983). In particular, the occurrence of the type I spectral change has been associated with a modulation of the ferric iron spin state equilibrium from low-spin to high-spin, accompanying substrate binding, enabling a calculation of the percentage high-spin content and the equilibrium constant for the process, from which thermodynamic data can be obtained. Specifically, a type I spectral change entails a reduction in the Soret absorption at 420 nm and a concomitant increase in the 390 nm absorption, which may be regarded as a shift in the hemoprotein spin equilibrium from low-spin to high-spin ferric P450.

1983). In particular, the occurrence of the type I spectral change has been associated with a modulation of the ferric iron spin state equilibrium from low-spin to high-spin, accompanying substrate binding, enabling a calculation of the percentage high-spin content and the equilibrium constant for the process, from which thermodynamic data can be obtained. Specifically, a type I spectral change entails a reduction in the Soret absorption at 420 nm and a concomitant increase in the 390 nm absorption, which may be regarded as a shift in the hemoprotein spin equilibrium from low-spin to high-spin ferric P450.

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