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Article

Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme C.

Biopolymers - 1 Jan 2001

Howes B D, Heering H A, Roberts T O, Schneider-Belhadadd F, Smith A T, Smulevich G

Abstract excerpt

Aromatic substrate binding to peroxidases is mediated through hydrophobic and hydrogen bonding interactions between residues on the distal side of the heme and the substrate molecule. The effects of perturbing these interactions are investigated by an electronic absorption and resonance Raman study of benzohydroxamic acid (BHA) binding to a series of mutants of horseradish peroxidase isoenzyme C (HRPC). In...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 11745121
DOI: 10.1002/bip.1021

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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