Magnetic Resonance Study of the Structure and Functions of Cytochrome P45

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Abstract
Cytochrome P450 is a membrane-bound enzyme providing oxidation of numerous organic compounds in organisms. The objective of this review is to show the wide possibilities that are provided by Electron Spin Resonance (ESR) and Nuclear Magnetic Resonance (NMR) techniques to the study of the structure and functions of this unique enzyme. High sensitivity of ESR spectra of cytochrome P450 to its functional state and interaction with substrates and inhibitors is illustrated. NMR and proton relaxation make it possible to obtain unique information about the structure of the active center of cytochrome P450 under physiological conditions. ESR and NMR methods allow one to obtain structural data on location of substrates, inhibitors, and their spin-labeled analogs with respect to Fe3+ ions in the enzyme-active center. Of special interest seems to be coupling of ESR with the affinity modification method. For this purpose, the spin-labeled analogs of cytochrome P450 substrates containing alkylating groups were used. As a result, an important datum has been obtained on the structure of active centers of cytochrome P450 in microsomes and in a highly purified state. In conclusion, the problems of the structure and functions of cytochrome P450, which can be most efficiently resolved with the use of magnetic resonance methods, are discussed.

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