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Structure and function of haemoglobins


Gell, DA, Structure and function of haemoglobins, Blood Cells, Molecules, and Diseases, 70 pp. 13-42. ISSN 1079-9796 (2018) [Refereed Article]

DOI: doi:10.1016/j.bcmd.2017.10.006


Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential for O2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a large family of Hb proteins with members distributed across all three domains of lifeā€"bacteria, archaea and eukaryotes. This review, aimed chiefly at researchers new to the field, attempts a broad overview of the diversity, and common features, in Hb structure and function. Topics include structural and functional classification of Hbs; principles of O2 binding affinity and selectivity between O2 /NO/CO and other small ligands; hexacoordinate (containing bis-imidazole coordinated haem) Hbs; bacterial truncated Hbs; flavohaemoglobins; enzymatic reactions of Hbs with bioactive gases, particularly NO, and protection from nitrosative stress; and, sensor Hbs. A final section sketches the evolution of work on the structural basis for allosteric O 2 binding by mammalian RBC Hb, including the development of newer kinetic models. Where possible, reference to historical works is included, in order to provide context for current advances in Hb research.

Item Details

Item Type:Refereed Article
Keywords:haemoglobin, myoglobin, truncated haemoglobin
Research Division:Biomedical and Clinical Sciences
Research Group:Cardiovascular medicine and haematology
Research Field:Haematology
Objective Division:Expanding Knowledge
Objective Group:Expanding knowledge
Objective Field:Expanding knowledge in the health sciences
UTAS Author:Gell, DA (Dr David Gell)
ID Code:151432
Year Published:2018
Web of Science® Times Cited:60
Deposited By:Plant Science
Deposited On:2022-07-28
Last Modified:2022-07-28

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