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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 d...

Topics

Animals
Binding Sites
Directed Molecular Evolution
Electrochemistry
Genetic Variation
Heme
Horses
Hydrogen Peroxide
In Vitro Techniques
Kinetics
Ligands
Membrane Potentials

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Myocardium

Myoglobin

Peroxidases

Spectrophotometry

Spectroscopy, Fourier Transform Infrared

Source

Identifiers

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

Genes

SHE

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9661283-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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