Editing Globin (section)

== Examples ==

Human genes encoding globin proteins include:
* [[Cytoglobin|CYGB]]
* [[Hemoglobin, alpha 1|HBA1]], [[HBA2]], [[HBB]], [[HBD]], [[HBE1]], [[HBG1]], [[HBG2]], [[mu hemoglobin|HBM]], [[HBQ1]], [[Hemoglobin subunit zeta|HBZ]], [[myoglobin|MB]]

The globins include:

*[[Haemoglobin]] (Hb)
*[[Myoglobin]] (Mb)
* [[Neuroglobin]]: a myoglobin-like haemprotein [[gene expression|expressed]] in vertebrate [[brain]] and retina, where it is involved in neuroprotection from damage due to [[Hypoxia (medical)|hypoxia]] or [[ischemia]].<ref name="pmid12962627">{{cite journal |vauthors=Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M | title = Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity | journal = Structure | volume = 11 | issue = 9 | pages = 1087–95 |date=September 2003 | pmid = 12962627 | doi = 10.1016/S0969-2126(03)00166-7| doi-access = free | hdl = 10067/455310151162165141 | hdl-access = free }}</ref> Neuroglobin belongs to a branch of the globin family that diverged early in [[evolution]].
*[[Cytoglobin]]: an oxygen sensor [[Gene expression|expressed]] in multiple [[Biological tissue|tissues]]. Related to neuroglobin.<ref name="pmid15804833">{{cite journal |vauthors=Fago A, Hundahl C, Malte H, Weber RE | title = Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins | journal = IUBMB Life | volume = 56 | issue = 11–12 | pages = 689–96 | year = 2004 | pmid = 15804833 | doi = 10.1080/15216540500037299 | s2cid = 21182182 | doi-access = free }}</ref>
*[[Erythrocruorin]]: highly cooperative [[extracellular]] respiratory [[proteins]] found in [[annelid]]s and [[arthropod]]s that are assembled from as many as 180 subunit into hexagonal bilayers.<ref name="pmid17084861">{{cite journal |vauthors=Royer WE, Omartian MN, Knapp JE | title = Low resolution crystal structure of Arenicola erythrocruorin: influence of coiled coils on the architecture of a megadalton respiratory protein | journal = J. Mol. Biol. | volume = 365 | issue = 1 | pages = 226–36 |date=January 2007 | pmid = 17084861 | pmc = 1847385 | doi = 10.1016/j.jmb.2006.10.016 }}</ref>
*[[Leghaemoglobin]] (legHb or [[symbiosis|symbiotic]] Hb): occurs in the [[root nodule]]s 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]] .
*[[Flavohaemoglobin]]s (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 [[electron]]s to haem in the globin.<ref name="pmid11092893">{{cite journal |vauthors=Mukai M, Mills CE, Poole RK, Yeh SR | title = Flavohemoglobin, a globin with a peroxidase-like catalytic site | journal = J. Biol. Chem. | volume = 276 | issue = 10 | pages = 7272–7 |date=March 2001 | pmid = 11092893 | doi = 10.1074/jbc.M009280200 | doi-access = free }}</ref>
*Globin E: a globin responsible for storing and delivering oxygen to the retina in birds<ref>{{cite journal |vauthors=Blank M, Kiger L, Thielebein A, Gerlach F, Hankeln T, Marden MC, Burmeister T |title= Oxygen supply from the bird's eye perspective: Globin E is a respiratory protein in the chicken retina |journal= J. Biol. Chem. |volume=286|issue=30|pages=26507–15|year=2011|pmid=21622558|doi= 10.1074/jbc.M111.224634|url=https://www.sciencedaily.com/releases/2011/06/110623130749.htm |pmc=3143615|doi-access= free }}</ref>
*Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the [[cytoplasm]]ic [[cell signalling|signalling]] domain of [[bacteria]]l chemoreceptors. They [[molecular binding|bind]] oxygen, and act to initiate an aerotactic response or [[Transcriptional regulation|regulate]] [[gene expression]].<ref name="pmid11481493">{{cite journal |vauthors=Hou S, Freitas T, Larsen RW, Piatibratov M, Sivozhelezov V, Yamamoto A, Meleshkevitch EA, Zimmer M, Ordal GW, Alam M | title = Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 16 | pages = 9353–8 |date=July 2001 | pmid = 11481493 | pmc = 55424 | doi = 10.1073/pnas.161185598 | bibcode = 2001PNAS...98.9353H | doi-access = free }}</ref><ref name="pmid15598488">{{cite journal |vauthors=Freitas TA, Saito JA, Hou S, Alam M | title = Globin-coupled sensors, protoglobins, and the last universal common ancestor | journal = J. Inorg. Biochem. | volume = 99 | issue = 1 | pages = 23–33 |date=January 2005 | pmid = 15598488 | doi = 10.1016/j.jinorgbio.2004.10.024 }}</ref>
*[[Protoglobin]]: a single domain globin found in [[archaea]] that is related to the N-terminal domain of globin-coupled sensors.<ref name="pmid15096613">{{cite journal |vauthors=Freitas TA, Hou S, Dioum EM, Saito JA, Newhouse J, Gonzalez G, Gilles-Gonzalez MA, Alam M | title = Ancestral hemoglobins in Archaea | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 17 | pages = 6675–80 |date=April 2004 | pmid = 15096613 | pmc = 404104 | doi = 10.1073/pnas.0308657101 | bibcode = 2004PNAS..101.6675F | doi-access = free }}</ref>
*Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 [[alpha helix|alpha-helical]] sandwich [[protein folding|fold]]. Can be divided into three main groups (I, II and II) based on [[secondary structure|structural]] features.
*HbN (or GlbN): a truncated haemoglobin-like protein that binds oxygen cooperatively with a very high affinity and a slow [[Dissociation (chemistry)|dissociation]] rate, which may exclude it from oxygen transport. It appears to be involved in [[bacterial]] nitric oxide [[detoxification]] and in nitrosative [[Stress (medicine)|stress]].<ref name="pmid16814781">{{cite journal |vauthors=Lama A, Pawaria S, Dikshit KL | title = Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis | journal = FEBS Lett. | volume = 580 | issue = 17 | pages = 4031–41 |date=July 2006 | pmid = 16814781 | doi = 10.1016/j.febslet.2006.06.037 | doi-access = free }}</ref>
*[[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.<ref name="pmid10684619">{{cite journal |vauthors=Yeh DC, Thorsteinsson MV, Bevan DR, Potts M, La Mar GN | title = Solution 1H NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune | journal = Biochemistry | volume = 39 | issue = 6 | pages = 1389–99 |date=February 2000 | pmid = 10684619 | doi = 10.1021/bi992081l}}</ref>
*HbO (or GlbO): a truncated haemoglobin-like protein with a lower oxygen affinity than HbN. HbO associates with the bacterial [[cell (biology)|cell]] membrane, where it [[statistical significance|significantly]] increases oxygen uptake over [[Cell membrane|membrane]]s lacking this protein. HbO appears to [[protein–protein interaction|interact]] with a terminal oxidase, and could participate in an oxygen/electron-transfer process that facilitates oxygen transfer during [[aerobic metabolism]].<ref name="pmid11796724">{{cite journal |vauthors=Pathania R, Navani NK, Rajamohan G, Dikshit KL | title = Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli | journal = J. Biol. Chem. | volume = 277 | issue = 18 | pages = 15293–302 |date=May 2002 | pmid = 11796724 | doi = 10.1074/jbc.M111478200 | doi-access = free }}</ref>
*Glb3: a nuclear-encoded truncated haemoglobin from [[plant]]s 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]].<ref name="pmid11526234">{{cite journal |vauthors=Watts RA, Hunt PW, Hvitved AN, Hargrove MS, Peacock WJ, Dennis ES | title = A hemoglobin from plants homologous to truncated hemoglobins of microorganisms | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 98 | issue = 18 | pages = 10119–24 |date=August 2001 | pmid = 11526234 | pmc = 56925 | doi = 10.1073/pnas.191349198 | bibcode = 2001PNAS...9810119W | doi-access = free }}</ref>