| Description | Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [ ]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric globins, flavohaemoglobins and globin-coupled sensors. Bacteria have all three types of globins, while archaea lack flavohaemoglobins, and eukaryotes lack globin-coupled sensors []. Several functionally different haemoglobins can coexist in the same species. The major types of globins include:Haemoglobin (Hb): tetramer of two alpha and two beta chains, although embryonic and foetal forms can substitute the alpha or beta chain for ones with higher oxygen affinity, such as gamma, delta, epsilon or zeta chains. Hb transports oxygen from lungs to other tissues in vertebrates [ ]. Hb proteins are also present in unicellular organisms where they act as enzymes or sensors [].Myoglobin (Mb): monomeric protein responsible for oxygen storage in vertebrate muscle [ ].Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia [ ]. Neuroglobin belongs to a branch of the globin family that diverged early in evolution.Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to neuroglobin [ ].Erythrocruorin: highly cooperative extracellular respiratory proteins found in annelids and arthropods that are assembled from as many as 180 subunit into hexagonal bilayers [ ].Leghaemoglobin (legHb or symbiotic Hb): occurs in the root nodules of leguminous plants, where it facilitates the diffusion of oxygen to symbiotic bacteriods in order to promote nitrogen fixation.Non-symbiotic haemoglobin (NsHb): occurs in non-leguminous plants, and can be over-expressed in stressed plants [ ].Flavohaemoglobins (FHb): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD/FAD-binding domain. FHb provides protection against nitric oxide via its C-terminal domain, which transfers electrons to haem in the globin [ ].Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the cytoplasmic signalling domain of bacterial chemoreceptors. They bind oxygen, and act to initiate an aerotactic response or regulate gene expression [ , ].Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors [ ].Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 α-helical sandwich fold. Can be divided into three main groups (I, II and II) based on structural features [ ].This entry represents trematode type myoglobin. Trematodes are the parasitic worms inhabiting various body organs of vertebrates where oxygen might be scarce or intermittent, as in the bile ducts or stomach of ruminants or the swim bladder of fishes. Trematodes possess a cytoplasmic oxygen-binding hemoprotein of ~17kDa [ ] distributed throughout the body. The absorption spectrum shows the presence of haem (Fe-protoporphyrin IX) as a prosthetic group in the globin []. Unlike human Hb, the trematode oxygen-binding haemoproteins are monomeric and are not involved in the transport of oxygen within a circulatory system. High oxygen affinity molecules would not release the oxygen rapidly. The trematodes have a tyrosine in position B10; two H-bonds from this to the oxygen molecule are thought to be responsible for the very high oxygen affinity. The trematode haemoglobins display a combination of high association rates and very low dissociation rates, resulting in some of the highest oxygen affinities ever observed []. | Name | Globin, trematode |
| Short Name | Globin_trematode | Type | Family |
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