Comparison of aniline hydroxylation by hemoglobin and microsomal cytochrome P450 using stable isotopes

Add time:08/19/2019    Source:sciencedirect.com

Hemoglobin (Hb) and cytochrome P450 carry out aromatic ring hydroxylation of aniline. In the presence of reductants and Hb, para- and ortho-aminophenol were formed. Under [18O]O2, 100% of product was labeled; no incorporation occurred with [18O]H2O. Deuterium (1.9%) was detectable in p-aminophenol formed from p-[2H]aniline by Hb, as compared with 6% retention observed with cytochrome P450. These observations are consistent with a mechanism for Hb-dependent reaction involving formation of an ironoxo complex competent to hydroxylate substrate. Hb-mediated reactions may represent a source of extrahepatic metabolism since Hb is a major carrier for small organic molecules. The similarities of P450- and Hb-mediated aniline hydroxylation using stable isotopes preclude their use as in vivo probes.

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