Activation of Oxygen by Cytochrome P-450 and Other Haemoproteins

Data on the activation of molecular oxygen by the full microsomal hydroxylating system containing cytochrome P-450 as the terminal oxygenase are examined. The nature of the hydroxylating agent, which is the oxenoid Fe³⁺O, is analysed. The autoxidation reactions of cytochrome P-450 from various sources, haemoglobin, myoglobin, and peroxidases are compared and the role of the axial ligands of the haem iron and the structure of the active centres of the haemoproteins in this process is demonstrated. The possible mechanisms of the oxidation of organic compounds by peroxides with participation of cytochrome P-450, cytochrome c, haemoglobin, and catalase are examined critically. Haemoproteins have been divided into three groups in terms of the type of peroxide oxidation reactions. The relative contributions of the radical and two-electron reactions in the oxidation of compounds by peroxides with participation of different haemoproteins are analysed.
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