Leghaemoglobin, iron-binding site
Short name | Leghaemoglobin_Fe_BS |
Description
* 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
* 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
* 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
* Anaerobic nitrite reductase: phytoglobin that reduces nitrite to nitric oxide (NO) under anoxic conditions
References
1.Plant hemoglobins: what we know six decades after their discovery. Garrocho-Villegas V, Gopalasubramaniam SK, Arredondo-Peter R. Gene 398, 78-85, (2007). View articlePMID: 17540516
2.Protein structure in the truncated (2/2) hemoglobin family. Pesce A, Nardini M, Milani M, Bolognesi M. IUBMB Life 59, 535-41, (2007). View articlePMID: 17701548
3.A model of globin evolution. Vinogradov SN, Hoogewijs D, Bailly X, Mizuguchi K, Dewilde S, Moens L, Vanfleteren JR. Gene 398, 132-42, (2007). View articlePMID: 17540514
4.A phylogenomic profile of globins. Vinogradov SN, Hoogewijs D, Bailly X, Arredondo-Peter R, Gough J, Dewilde S, Moens L, Vanfleteren JR. BMC Evol. Biol. 6, 31, (2006). View articlePMID: 16600051
5.Sequential analysis of alpha- and beta-globin gene expression during erythropoietic differentiation from primate embryonic stem cells. Umeda K, Heike T, Nakata-Hizume M, Niwa A, Arai M, Shinoda G, Ma F, Suemori H, Luo HY, Chui DH, Torii R, Shibuya M, Nakatsuji N, Nakahata T. Stem Cells 24, 2627-36, (2006). View articlePMID: 16888280
6.Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy. Egawa T, Yeh SR. J. Inorg. Biochem. 99, 72-96, (2005). View articlePMID: 15598493
7.Myoglobin: an essential hemoprotein in striated muscle. Ordway GA, Garry DJ. J. Exp. Biol. 207, 3441-6, (2004). View articlePMID: 15339940
8.Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M. Structure 11, 1087-95, (2003). View articlePMID: 12962627
9.Functional properties of neuroglobin and cytoglobin. Insights into the ancestral physiological roles of globins. Fago A, Hundahl C, Malte H, Weber RE. IUBMB Life 56, 689-96, (2004). PMID: 15804833
10.Low resolution crystal structure of Arenicola erythrocruorin: influence of coiled coils on the architecture of a megadalton respiratory protein. Royer WE Jr, Omartian MN, Knapp JE. J. Mol. Biol. 365, 226-36, (2007). View articlePMID: 17084861
11.Flavohemoglobin, a globin with a peroxidase-like catalytic site. Mukai M, Mills CE, Poole RK, Yeh SR. J. Biol. Chem. 276, 7272-7, (2001). View articlePMID: 11092893
12.Globin-coupled sensors: a class of heme-containing sensors in Archaea and Bacteria. Hou S, Freitas T, Larsen RW, Piatibratov M, Sivozhelezov V, Yamamoto A, Meleshkevitch EA, Zimmer M, Ordal GW, Alam M. Proc. Natl. Acad. Sci. U.S.A. 98, 9353-8, (2001). View articlePMID: 11481493
13.Globin-coupled sensors, protoglobins, and the last universal common ancestor. Freitas TA, Saito JA, Hou S, Alam M. J. Inorg. Biochem. 99, 23-33, (2005). View articlePMID: 15598488
14.Ancestral hemoglobins in Archaea. Freitas TA, Hou S, Dioum EM, Saito JA, Newhouse J, Gonzalez G, Gilles-Gonzalez MA, Alam M. Proc. Natl. Acad. Sci. U.S.A. 101, 6675-80, (2004). View articlePMID: 15096613
15.Legume haemoglobins: symbiotic nitrogen fixation needs bloody nodules. Downie JA. Curr. Biol. 15, R196-8, (2005). View articlePMID: 15797009
16.Plants, humans and hemoglobins. Kundu S, Trent JT 3rd, Hargrove MS. Trends Plant Sci. 8, 387-93, (2003). View articlePMID: 12927972
17.The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme. Kundu S, Snyder B, Das K, Chowdhury P, Park J, Petrich JW, Hargrove MS. Proteins 46, 268-77, (2002). View articlePMID: 11835502
18.[Study on the serum concentrations of gentamicin after intravenous drip infusion] Shiramatsu K, Ishida K, Takahashi K, Kunimoto M, Denno R, Akiyama M, Hirata K, Hayasaka H. 36, 293-8, (1983). PMID: 6854938
19.Modulation of nitric oxide bioactivity by plant haemoglobins. Perazzolli M, Romero-Puertas MC, Delledonne M. J. Exp. Bot. 57, 479-88, (2006). View articlePMID: 16377734
20.Plant and cyanobacterial hemoglobins reduce nitrite to nitric oxide under anoxic conditions. Sturms R, DiSpirito AA, Hargrove MS. Biochemistry 50, 3873-8, (2011). View articlePMID: 21495624
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- PROSITE patterns:PS00208