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Article

An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate.

Biochemistry - 21 Dec 2010

Yuan Yue, Simplaceanu Virgil, Ho Nancy T, Ho Chien

Abstract excerpt

On the basis of X-ray crystal structures and electron paramagnetic resonance (EPR) measurements, it has been inferred that the O(2) binding to hemoglobin is stabilized by the hydrogen bonds between the oxygen ligands and the distal histidines. Our previous study by multinuclear nuclear magnetic resonance (NMR) spectroscopy has provided the first direct evidence of such H-bonds in human normal adult oxyhemoglobin...

Topics

Humans
Hydrogen Bonding
Hydrogen-Ion Concentration
Models, Molecular
Mutation
Oxyhemoglobins
Phytic Acid
Temperature

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 21077639
DOI: 10.1021/bi100927p
PMCID: PMC3033742

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-21077639-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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