Possible higher valence states of cytochrome P-450 during oxidative reactions |
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Authors: | A D Rahimtula P J O'Brien E G Hrycay J A Peterson R W Estabrook |
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Affiliation: | 1. Department of Biochemistry Memorial University of Newfoundland St. Johns, Newfoundland, Canada;2. Department of Biochemistry The University of Texas Health Science Center Dallas, Texas, USA |
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Abstract: | The addition of the organic hydroperoxide, cumene hydroperoxide, to liver microsomes results in the appearance of a transient spectral change associated with cytochrome P-450. In addition, unique electron paramagnetic resonance signals are observed with liver microsomal cytochrome P-450 comparable to signals obtained when peroxides interact with metmyoglobin. It is suggested that higher valence states of cytochrome P-450 may function during the activation of oxygen for the hydroxylation of a variety of xenobiotics. |
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