By David F.V. Lewis
This consultant to the constitution, functionality and mechanism of the cytochromes P450 specializes in the function of P450s in xenobiotic metabolism and toxicity. color illustrations express how modelling of P450s can rationalize their substrate specificity for the metabolism of either endogenous and exogenous chemical compounds.
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Additional info for Cytochromes P450: Structure, Function and Mechanism (Taylor & Francis Series in Pharmaceutical Sciences)
1989). The characteristic 15N chemical shift of isotopicallylabelled CN– in these complexes varies in accordance with the electronic environment of the heme, indicating that substrate binding increases the electron density on the iron atom, whereas putidaredoxin binding brings about a decrease in electron spin density, which are thought to reflect the influence of the thiolate ligand on these two stages in the P450cam catalytic cycle. , 1980). However, the supposition that histidine may be the fifth ligand has been discounted, as it is now regarded that the ENDOR coupling observed was due to the porphyrin ring nitrogens (Hawkins and Dawson, 1992).
12 Vibrational modes in metal porphyrins (Reference: Lewis, 1986) In-plane vibrations No. of modes Out-of-plane vibrations No. , 1976) and crystallographic evidence from the P450camCO complex does indeed show that there is significant non-linearity in the Fe−CO moiety (Raag and Poulos, 1989a) which is at an angle of 166° in the solid state structure. 5). 5 Linear relationship between oxygen-oxygen stretching frequencies and bond energies for O2, species. 21 and example, super oxide shows an absorption between 1100 cm–1 and 1150 cm–1, whereas free dioxygen absorbs at about 1555 cm–1, and peroxide has an IR stretching frequency around 850 cm–1 (Lewis, 1986).
The resulting changes in the CD spectra of both P450LM2 and P450LM4 following treatment with detergent were reported to be indicative of an increase in -helical content of the protein (Chiang and Coon, 1979). , 1983) which was found to be the same as that of hemoglobin. More recently, MCD and other spectroscopic techniques have been used to compare the different heme-thiolate proteins, P450 and chloroperoxidase (Dawson and Sono, 1987), heme-containing oxygenases and peroxidases (Dawson, 1988), and P450 with secondary amine oxidase (Hawkins and Dawson, 1992).
Cytochromes P450: Structure, Function and Mechanism (Taylor & Francis Series in Pharmaceutical Sciences) by David F.V. Lewis