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Article

Monooxygenation of an aromatic ring by F43W/H64D/V68I myoglobin mutant and hydrogen peroxide. Myoglobin mutants as a model for P450 hydroxylation chemistry.

The Journal of biological chemistry - 1 Apr 2005

Pfister Thomas D, Ohki Takahiro, Ueno Takafumi, Hara Isao, Adachi Seiji, Makino Yumiko, Ueyama Norikazu, Lu Yi, Watanabe Yoshihito

Abstract excerpt

Myoglobin (Mb) is used as a model system for other heme proteins and the reactions they catalyze. The latest novel function to be proposed for myoglobin is a P450 type hydroxylation activity of aromatic carbons (Watanabe, Y., and Ueno, T. (2003) Bull. Chem. Soc. Jpn. 76, 1309-1322). Because Mb does not contain a specific substrate binding site for aromatic compounds near the heme, an engineered tryptophan in the...

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PMID: 15664991
DOI: 10.1074/jbc.M410853200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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