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Article

Spectroscopic and functional studies of a novel quadruple myoglobin variant with increased peroxidase activity.

Journal of inorganic biochemistry - 1 Apr 1998

Hildebrand D P, Lim K T, Rosell F I, Twitchett M B, Wan L, Mauk A G

Abstract excerpt

A quadruple variant of horse heart myoglobin (Thr39Ile/Lys45Asp/Phe46Leu/Ile107Phe) that exhibits significantly (approximately 25-fold) greater peroxidase activity than the wild-type protein has been studied to determine its midpoint reduction potential (24(2) mV vs. SHE; pH 6.0, mu = 0.1 M, 25 degrees C) and to characterize the kinetics of its reaction with hydrogen peroxide. In addition, Fourier transform...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 9661283
DOI: 10.1016/s0162-0134(98)00007-5

Genes

SHE

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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