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Article

Oxidative modification of tryptophan 43 in the heme vicinity of the F43W/H64L myoglobin mutant.

The Journal of biological chemistry - 28 Sept 2001

Hara I, Ueno T, Ozaki Si, Itoh S, Lee K, Ueyama N, Watanabe Y

Abstract excerpt

The F43W/H64L myoglobin mutant was previously constructed to investigate the effects of electron-rich tryptophan residue in the heme vicinity on the catalysis, where we found that Trp-43 in the mutant was oxidatively modified in the reaction with m-chloroperbenzoic acid (mCPBA). To identify the exact structure of the modified tryptophan in this study, the mCPBA-treated F43W/H64L mutant has been digested stepwise...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11481319
DOI: 10.1074/jbc.C100371200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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