Rescue of the horseradish peroxidase His-170-->Ala mutant activity by imidazole: importance of proximal ligand tethering.

doi:10.1021/bi9609331

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Article

Rescue of the horseradish peroxidase His-170-->Ala mutant activity by imidazole: importance of proximal ligand tethering.

Biochemistry - 1 Oct 1996

Newmyer S L, Sun J, Loehr T M, Ortiz de Montellano P R

Abstract excerpt

The proximal iron ligand in horseradish peroxidase (HRP) is His-170. The H170A mutant of polyhistidine-tagged HRP (hHRP) has been expressed in a baculovirus system and has been purified and characterized. At pH 7, the Soret maximum of the mutant is at 414 nm rather than 403 nm. Resonance Raman sp...

Topics

Baculoviridae
Benzothiazoles
Enzyme Activation
Escherichia coli
Guaiacol
Hemeproteins
Histidine
Horseradish Peroxidase
Hydrogen Peroxide
Hydrogen-Ion Concentration
Imidazoles
Iron
Kinetics
Mutation
Protein Binding
Recombinant Proteins
Spectrum Analysis, Raman
Sulfonic Acids

Source

Open in PubMed

Identifiers

PMID: 8841121
DOI: 10.1021/bi9609331

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8841121-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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