| Description | This entry represents a group of haemoglobin-like proteins found in eubacteria, cyanobacteria, protozoa, algae and plants, but not in animals or yeast. These proteins have a truncated 2-over-2 rather than the canonical 3-over-3 α-helical sandwich fold [ ]. They include:HbN (or GlbN): a truncated haemoglobin-like protein that binds oxygen cooperatively with a very high affinity and a slow dissociation rate, which may exclude it from oxygen transport. It appears to be involved in bacterial nitric oxide detoxification and in nitrosative stress [ ].Cyanoglobin (or GlbN): a truncated haemoprotein found in cyanobacteria that has high oxygen affinity, and which appears to serve as part of a terminal oxidase, rather than as a respiratory pigment [ ].HbO (or GlbO): a truncated haemoglobin-like protein with a lower oxygen affinity than HbN. HbO associates with the bacterial cell membrane, where it significantly increases oxygen uptake over membranes lacking this protein. HbO appears to interact with a terminal oxidase, and could participate in an oxygen/electron-transfer process that facilitates oxygen transfer during aerobic metabolism [ ].Glb3: a nuclear-encoded truncated haemoglobin from plants that appears more closely related to HbO than HbN. Glb3 from Arabidopsis thaliana (Mouse-ear cress) exhibits an unusual concentration-independent binding of oxygen and carbon dioxide [ ].The truncated haemoglobin (trHb) family branches into three main groups, designated as type I, II and III and named as HbN, HbO and HbP, respectively. The trHbO gene (also known as glbO) has been predicted as the ancestral gene, with group I and group III genes appearing as a result of duplication and transfer events. There is an accumulating evidence suggests that trHbs may be implicated in functions other than oxygen delivery [ ]. | Name | Truncated hemoglobin |
| Short Name | Hemoglobin_trunc | Type | Family |
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