Horseradish peroxidase Phe172-->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical.

doi:10.1074/jbc.270.31.18413

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Horseradish peroxidase Phe172-->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical.

The Journal of biological chemistry - 4 Aug 1995

Miller V P, Goodin D B, Friedman A E, Hartmann C, Ortiz de Montellano P R

Abstract excerpt

A gene coding for the F172Y mutant of horseradish peroxidase isozyme C (HRP) has been constructed and expressed in both Spodoptera frugiperda (SF-9) and Trichoplusia ni egg cell homogenate (HighFive) cells. Homology modeling with respect to three peroxidases for which crystal structures are available places Phe172 on the proximal side of the heme in the vicinity of porphyrin pyrrole ring C. The pH optimum and...

Topics

Animals
Baculoviridae
Base Sequence
Binding Sites
Cations
Cells, Cultured
Electron Spin Resonance Spectroscopy
Free Radicals
Guaiacol
Heme
Horseradish Peroxidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydrogen Peroxide

Hydrogen-Ion Concentration

Isoenzymes

Kinetics

Molecular Sequence Data

Mutagenesis, Site-Directed

Mutation

Source

Open in PubMed

Identifiers

PMID: 7629167
DOI: 10.1074/jbc.270.31.18413

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7629167-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Horseradish peroxidase Phe172-->Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical.PMID 7629167Read ↗

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

Detection of a tryptophan radical as an intermediate species in the reaction of horseradish peroxidase mutant (Phe-221 --> Trp) and hydrogen peroxide.Semantic proximity Read ↗

Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates.Semantic proximity Read ↗

Characterization of the hydrogen peroxide-enzyme reaction for two cytochrome c peroxidase mutants.Semantic proximity Read ↗

Using an artificial tryptophan "wire" in cytochrome c peroxidase for oxidation of organic substrates.Semantic proximity Read ↗

Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.Semantic proximity Read ↗

Multifrequency high-field EPR study of the tryptophanyl and tyrosyl radical intermediates in wild-type and the W191G mutant of cytochrome c peroxidase.Semantic proximity Read ↗

Identification of a critical phenylalanine residue in horseradish peroxidase, Phe179, by site-directed mutagenesis and 1H-NMR: implications for complex formation with aromatic donor molecules.Semantic proximity Read ↗

Modulation of redox potential and alteration in reactivity via the peroxide shunt pathway by mutation of cytochrome P450 around the proximal heme ligand.Semantic proximity Read ↗

Horseradish peroxidase mutants that autocatalytically modify their prosthetic heme group: insights into mammalian peroxidase heme-protein covalent bonds.Semantic proximity Read ↗

Role of electrostatics and salt bridges in stabilizing the compound I radical in ascorbate peroxidase.Semantic proximity Read ↗

Development of an improved Amplex Red peroxidation activity assay for screening cytochrome P450 variants and identification of a novel mutant of the thermophilic CYP119.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.