CYGB binds O2

Stable Identifier
Reaction [binding]
Homo sapiens
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Vertebrates possess multiple respiratory globins that differ in structure, function, and tissue distribution. Three different globins have been described so far: hemoglobin facilitates oxygen transport in blood, myoglobin mediates oxygen transport and storage in the muscle and neuroglobin has a yet unidentified function in nerve cells. A fourth globin has been identified in mouse, human and zebrafish. It is ubiquitously expressed in human tissue and therefore called cytoglobin (CYGB) (Burmester et al. 2002, Trent & Hargrove 2002). Unlike the specific expression patterns of Hb and Mb, CYGB is found in vascular smooth muscle, fibroblasts and cardiomyocytes. CYGB functions as a homodimer (Hamdane et al. 2003) and is localised to the cytosol of these cells where its O2 loading and unloading ability within a narrow O2 tension range makes it an ideal protein for O2 storage, especially during hypoxia (Fago et al. 2004).

Literature References
PubMed ID Title Journal Year
14530264 The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin

Hankeln, T, Burmester, T, Pesce, A, Hamdane, D, Bolognesi, M, Kiger, L, Marden, MC, Uzan, J, Dewilde, S, Moens, L, Green, BN

J. Biol. Chem. 2003
11893755 A ubiquitously expressed human hexacoordinate hemoglobin

Hargrove, MS, Trent, JT

J. Biol. Chem. 2002
15299006 Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance

Gilany, K, Hundahl, C, Dewilde, S, Moens, L, Fago, A, Weber, RE

J. Biol. Chem. 2004
11919282 Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues

Hankeln, T, Burmester, T, Ebner, B, Weich, B

Mol. Biol. Evol. 2002
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