@article{gell_structure_2017,
	title = {Structure and function of haemoglobins.},
	volume = {70},
	doi = {10.1016/j.bcmd.2017.10.006},
	abstract = {Abstract   Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential for O 2  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 O 2  binding affinity and selectivity between O 2 /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.},
	journal = {Blood Cells Molecules and Diseases},
	author = {Gell, David A.},
	month = oct,
	year = {2017},
	doi = {10.1016/j.bcmd.2017.10.006},
	pmid = {29126700},
	note = {MAG ID: 2765145472},
	pages = {13--42},
}

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