Abstract
Data on the activation of molecular oxygen by the full microsomal hydroxylating system containing cytochrome P-450 as theterminal oxygenase are examined. The nature of the hydroxylating agent, which is the oxenoid Fe3+O, is analysed. Theautoxidation reactions of cytochrome P-450 from various sources, haemoglobin, myoglobin, and peroxidases are comparedand the role of the axial ligands of the haem iron and the structure of the active centres of the haemoproteins in this processis demonstrated. The possible mechanisms of the oxidation of organic compounds by peroxides with participation of cytochromeP-450, cytochrome c, haemoglobin, and catalase are examined critically. Haemoproteins have been divided intothree groups in terms of the type of peroxide oxidation reactions. The relative contributions of the radical and two-electronreactions in the oxidation of compounds by peroxides with participation of different haemoproteins are analysed. The bibliography includes 184 references.
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