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Cited by 317Hemoglobin structure and functionHemoglobinopathies and Related DisordersProtein Interaction Studies and Fluorescence Analysis

Hemoglobin: Structure, Function and Allostery

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Ahmed, Mostafa H., Ghatge, Mohini S., Safo, Martin K.·2020·Subcellular Biochemistry
DOI 10.1007/978-3-030-41769-7_14PMC PMC7370311
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Abstract

This chapter reviews how allosteric (heterotrophic) effectors and natural mutations impact hemoglobin (Hb) primary physiological function of oxygen binding and transport. First, an introduction about the structure of Hb is provided, including the ensemble of tense and relaxed Hb states and the dynamic equilibrium of Hb multistate. This is followed by a brief review of Hb variants with altered Hb structure and oxygen binding properties. Finally, a review of different endogenous and exogenous allosteric effectors of Hb is presented with particular emphasis on the atomic interactions of synthetic ligands with altered allosteric function of Hb that could potentially be harnessed for the treatment of diseases.

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  • Increased avidity through multimerisation is well known, but it remains less well characterised in the context of transcription factor biology.

    “While increased avidity through multimerisation is well known (e.g. haemoglobin 69,70 ), it remains less well characterised in the context of TF biology 71 .”

    From Tetramerisation governs SALL transcription factor function in development and disease (2025) · cites this paper as [70]

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Cited by

Sorted by citations

Authors
Ahmed, M. H., Ghatge, M. S., & Safo, M. K.
Affiliations
Virginia Commonwealth University (US)
Corresponding author
Safo, Martin K.
ORCID
Venue
Subcellular Biochemistry
Publisher
Springer International Publishing
Published
2020
Volume
94
Pages
345-382
ISSN
  • 0306-0225 (ISSN-L)
  • 2542-8810
DOI
10.1007/978-3-030-41769-7_14
PMC
PMC7370311
OpenAlex
W3011621712
Cited by
317
References
202
Citations by year
2026: 65 · 2025: 72 · 2024: 63 · 2023: 60 · 2022: 34 · 2021: 21 · 2020: 2
FWCI
48.58
Type
book chapter
Language
en
Open access
Licence
www.springer.com/tdm (tdm)
Locations
  • Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health (1s10od021756-01a1)
  • National Institute on Minority Health and Health Disparities (R01MD009124)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
hemoglobin, allosteric regulation, oxygen binding, oxygen transport, hemoglobin variants, natural mutation, synthetic ligands, hemoglobin structure
MeSH terms
Allosteric Regulation, Hematologic Diseases, Hemoglobins, Humans, Ligands, Oxygen

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