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Peroxidation of a Specific Tryptophan of Metmyoglobin by Hydrogen Peroxide

Year: 1997

Type: article

Abstract: Globin-centered radicals at tyrosine and tryptophan residues and a peroxyl radical at an unknown location have been reported previously as products of the reaction of metmyoglobin with hydrogen peroxide. The peroxyl radical is shown here to be localized on tryptophan through the use of recombinant sperm whale myoglobin labeled with 13C at the indole ring C-3. Peroxyl radical formation was not prevented by site-directed mutations that replaced all three tyrosines, the distal histidine, or tryptophan 7 with non-oxidizable residues. In contrast, mutation of tryptophan 14 prevents peroxyl radical formation, implicating tryptophan 14 as the specific site of the peroxidation.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.272.4.2359

Authors: Janice A. DeGray, Michael R. Gunther, Richard Tschirret-Guth, Paul R. Ortiz de Montellano, Ronald P. Mason

Institutions: National Institutes of Health, National Institute of Environmental Health Sciences, University of California, San Francisco

Language: English

Topic: Hemoglobin structure and function

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W2056254096

FWCI: 3.834

Cites: 27

Cited by: 107

Related to: 10