FTIR analysis of the interaction of azide with horse heart myoglobin variants.

doi:10.1021/bi00190a013

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Article

FTIR analysis of the interaction of azide with horse heart myoglobin variants.

Biochemistry - 21 Jun 1994

Bogumil R, Hunter C L, Maurus R, Tang H L, Lee H, Lloyd E, Brayer G D, Smith M, Mauk A G

Abstract excerpt

The interaction of azide with variants of horse heart myoglobin (Mb) has been characterized by Fourier transform infrared (FTIR), electron paramagnetic resonance (EPR), and UV-VIS absorption spectroscopy and by molecular modeling calculations. Distal histidine variants (His64Thr, His64Ile, His64Lys) and charged surface variants (Val67Arg, Lys45Glu, Lys45Glu/Lys63Glu) were included in this study. All variants,...

Topics

Animals
Azides
Binding Sites
Electrochemistry
Electron Spin Resonance Spectroscopy
Heme
Histidine
Horses
Models, Molecular
Molecular Structure
Mutation
Myocardium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Myoglobin

Protein Binding

Recombinant Proteins

Spectrophotometry

Spectroscopy, Fourier Transform Infrared

Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 8011626
DOI: 10.1021/bi00190a013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8011626-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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