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Eur J Biochem. 1996 Aug 15;240(1):232-8.

Microperoxidase/H2O2-catalyzed aromatic hydroxylation proceeds by a cytochrome-P-450-type oxygen-transfer reaction mechanism.

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1
Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.

Abstract

The mechanism of aromatic hydroxylation of aniline and phenol derivatives in a H2O2-driven microperoxidase-8(MP8)-catalyzed reaction was investigated. It was shown that the reaction was not inhibited by the addition of scavengers of superoxide anion or hydroxyl radicals, which demonstrates that the reaction mechanism differs from that of the aromatic hydroxylation catalyzed by a horseradish peroxidase/ dihydroxyfumarate system. Additional experiments with 18O-labelled H2 18O2 demonstrated that the oxygen incorporated into aniline to give 4-aminophenol originates from H2O2. Furthermore, it was found that the addition of ascorbic acid efficiently blocks all peroxidase-type reactions that can be catalyzed by the MP8/H2O2 system, but does not inhibit the aromatic hydroxylation of aniline and phenol derivatives. Together, these observations exclude reaction mechanisms for the aromatic hydroxylation that proceed through peroxidase-type mechanisms in which the oxygen incorporated into the substrate originates from O2 or H2O. The mechanism instead seems to proceed by an initial attack of the high-valent iron-oxo intermediate of MP8 on the pi-electrons of the aromatic ring of the substrate leading to product formation by a cytochrome-P-450-type of sigma-O-addition or oxygen-rebound mechanism. This implies that MP8, which has a histidyl and not a cysteinate fifth axial ligand, is able to react by a cytochrome-P-450-like oxygen-transfer reaction mechanism.

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