Structure-Function Relations of Human Hemoglobins

Marengo-Rowe, Alain J.

doi:10.1080/08998280.2006.11928171

Cited by 179Hemoglobin structure and functionHemoglobinopathies and Related DisordersBlood properties and coagulation

Structure-Function Relations of Human Hemoglobins

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Marengo-Rowe, Alain J.·2006·Baylor University Medical Center Proceedings

DOI 10.1080/08998280.2006.11928171PMC PMC1484532

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Abstract

In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of smaller peptides, defined the molecular defect in HbS by showing that it differed from normal adult hemoglobin by only a single peptide. Since then, more than 200 variant and abnormal hemoglobins have been described. Furthermore, the construction of an atomic model of the hemoglobin molecule based on a high-resolution x-ray analysis by Dr. Max Perutz at Cambridge has permitted the study of the stereochemical part played by the amino acid residues, which were replaced, deleted, or added to in each of the hemoglobin variants. Some of the variants have been associated with clinical conditions. The demonstration of a molecular basis for a disease was a significant turning point in medicine. A new engineered hemoglobin derived from crocodile blood, with markedly reduced oxygen affinity and increased oxygen delivery to the tissues, points the way for future advances in medicine.

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The haem group contains iron as a co-factor at its core and the iron reversibly binds oxygen only when it is in the ferrous form (Fe2+).
“The haem group contains iron as a co-factor at its core and the iron reversibly binds oxygen only when it is in the ferrous form (Fe2+) (Marengo-Rowe, 2006).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Marengo-Rowe, 2006

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Authors: Marengo-Rowe, A. J.
Affiliations: Baylor University Medical Center (US)
Corresponding author: Marengo-Rowe, Alain J.
Venue: Baylor University Medical Center Proceedings
Publisher: Informa UK Limited
Published: 2006-07
Volume: 19
Issue: 3
Pages: 239-245
ISSN: 0899-8280 (ISSN-L)
1525-3252
DOI: 10.1080/08998280.2006.11928171
PMC: PMC1484532
OpenAlex: W1589718460
Cited by: 179
References: 54
Citations by year: 2026: 9 · 2025: 9 · 2024: 27 · 2023: 26 · 2022: 32 · 2021: 21 · 2020: 15 · 2019: 9 · 2018: 9 · 2017: 2 · 2016: 7 · 2015: 2 · 2014: 2 · 2013: 3 · 2012: 2
FWCI: 0.28
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Baylor University Medical Center Proceedings (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Blood properties and coagulation
Keywords: hemoglobin variants, hemoglobin S, structure-function relationship, amino acid substitutions, hemoglobinopathies, oxygen affinity, oxygen delivery

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Structure-Function Relations of Human Hemoglobins

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