Download Cytochromes P450: Structure, Function and Mechanism (Taylor by David F.V. Lewis PDF

By David F.V. Lewis

This consultant to the constitution, functionality and mechanism of the cytochromes P450 makes a speciality of the function 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 compounds.

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

Example text

19), are sensitive to the core size radius of the porphyrin ring and, consequently, can be used as core-size marker bands for the analysis of spin-state and coordination number (Spiro, 1983; Hildebrandt, 1992). 06 Å), that enable determination of the symmetry (C4v or D4h) of the heme environment, which can vary between 5-coordinate and 6-coordinate, and distinction between Fe(II) and Fe(III) in both high- and low-spin states. Although there are several other vibrational bands of lower frequency in the so-called ‘fingerprint’ region which have been assigned to a number of heme INTRODUCTION 25 vibrational modes, the iron-ligand absorption bands between 150 cm−1 and 500 cm−1 are important determinants of the heme coordination.

Such effects, caused by the porphyrin ring and the axial heme ligands, are common in hemoproteins and their ESR spectra have been characterized according to rhombicity and tetragonal field components (Blumberg and Peisach, 1971). 23). With percentage rhombicities* of around 26 per cent, P450s appear to be virtually unique in possessing the highest rhombicity values yet recorded for any hemoproteins. 0 that there is little similarity between these two families of enzymes. 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).

This is due to the fact that population of the MS±½ state falls exponentially with rise in temperature, thus bringing about dramatic reduction in the intensity of the resonant signals produced in the ESR spectrum. 0, respectively (Lewis, 1986). In cases where there are no rhombic distortions, such as in metmyoglobin, two ESR signals are observed with g values exactly corresponding to the aforementioned g values. The effects of rhombic and tetragonal distortions on the high-spin ferric system are essentially similar to those which operate for the low-spin case.

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