Myoglobin binds oxygen

Stable Identifier
R-HSA-8981606
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Myoglobin binds molecular oxygen (O2) in the cells of muscle tissue (Rossi-Fanelli and Antonini 1958, Boulton and Huntsman 1972, Wang et al. 2004). The dissociation constant of Myoglobin-oxygen is about 1 micromole per liter. The myoglobin:oxygen complex stores oxygen and also transports oxygen from the sarcolemma to the mitochondria. Myoglobin binds other small molecules such as nitric oxide and carbon monoxide. The ligands of myoglobin appear to migrate from the surface of the protein through pores (pockets) in the protein structure to reach the embedded heme group (reviewed in Tomita et al. 2010).
Literature References
PubMed ID Title Journal Year
5032105 Variants of human myoglobin: their oxygen dissociation curves

Boulton, FE, Huntsman, RG

Br. J. Haematol. 1972
15601759 Human myoglobin recognition of oxygen: dynamics of the energy landscape

Baskin, JS, Zewail, AH, Xia, T, Wang, Y

Proc. Natl. Acad. Sci. U.S.A. 2004
13584010 Studies on the oxygen and carbon monoxide equilibria of human myoglobin

ROSSI-FANELLI, A, ANTONINI, E

Arch. Biochem. Biophys. 1958
20675544 'It's hollow': the function of pores within myoglobin

Tomita, A, Jue, T, Kreutzer, U, Koshihara, SY, Adachi, S

J. Exp. Biol. 2010
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