University Of Tasmania

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Structure and function of haemoglobins

journal contribution
posted on 2023-05-21, 10:04 authored by David GellDavid Gell
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 life—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.


Publication title

Blood Cells, Molecules, and Diseases








Tasmanian School of Medicine


Academic Press Inc Elsevier Science

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525 B St, Ste 1900, San Diego, USA, Ca, 92101-4495

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Copyright 2017 Elsevier Inc

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Expanding knowledge in the health sciences

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