Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.

doi:10.1016/S0006-3495(93)81216-5

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Article

Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.

Biophysical journal - 1 Oct 1993

Gilch H, Schweitzer-Stenner R, Dreybrodt W

Abstract excerpt

We have examined the Fe(2+)-N epsilon (HisF8) complex in hemoglobin A (HbA) by measuring the band profile of its Raman-active nu Fe-His stretching mode at pH 6.4, 7.0, and 8.0 using the 441-nm line of a HeCd laser. A line shape analysis revealed that the band can be decomposed into five different...

Topics

Animals
Biophysical Phenomena
Biophysics
Hemoglobin A
Hemoglobins
Hemoglobins, Abnormal
Histidine
Horses
Humans
Iron
Models, Chemical
Molecular Structure

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Myoglobin

Photochemistry

Protein Conformation

Spectrum Analysis, Raman

Temperature

Source

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Identifiers

PMID: 8274641
DOI: 10.1016/S0006-3495(93)81216-5
PMCID: PMC1225874

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8274641-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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