The structure and function of mammalian and plant globins

Simon Brown, Yow Kong Soon


Globins are haemoproteins such as haemoglobin (Hb), myoglobin (Mb), cytoglobin (Cb), neuroglobin (Nb), leghaemoglobin (LHb) and non-symbiotic Hb (NsHb).  While the monomers of these six proteins have the characteristic ‘3-on-3’ alpha-helical sandwich tertiary structure and there are similarities in their patterns of secondary structure, they have poor primary sequence homology.  Moreover, they differ in quaternary structure and in the coordination of the haem, three (Hb, Mb, LHb) being 5-coordinate and Cb, Nb and NsHb being 6-coordinate.  Despite this, each of these globins binds small ligands, such as O2, CO and NO, in the sixth position, which implies that it must be possible to displace the imidazole occupying that position in Cb, Nb and NsHb.  In addition to O2 binding, globins are variously involved in O2 sensing and NO detoxification, and act as an NO dioxygenase.   These functions can generate the oxidised (or met-) form of the globin, which may be reduced by a globin reductase.  In the case of Hb two globin reductases have been characterised: a non-enzymatic reduction by cytochrome b5, which is enzymatically reduced by NADH:cytochrome b5 reductase, and an NADPH:flavin reductase.


chemistry; biology; globin; globin reductase; ligand binding; structure


The DOI for this article is: 10.12969/Scientia.Vol124.Sect2.Art05

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