Abstract
Myoglobin is a protein with a single hæme group, which binds oxygen inside our cells and makes it available for metabolism. Oxygen binding to myoglobin is described by a hyperbola. Hæmoglobin consists of two \(\upalpha\),\(\upbeta\)-protomers, each of the four proteins contains a hæme group. Binding of oxygen to one of these hæme groups increases the affinity of the remaining sites for oxygen; this cooperation results in an S-shaped (sigmoidal) binding curve. The shape of this curve is influenced by pH and the presence of 2,3-Bisphosphoglycerate (2,3-BPG). Mutations in the genes for either the \(\upalpha\)- or the \(\upbeta\)-subunits of hæmoglobin can cause serious disease.
Blood is a very special juice (J.W. v. Goethe: Faust I)
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Notes
- 1.
Named after Christian Bohr, physiologist and father of the physicist Niels Bohr.
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Buxbaum, E. (2015). Hæmoglobin and Myoglobin: Cooperativity. In: Fundamentals of Protein Structure and Function. Springer, Cham. https://doi.org/10.1007/978-3-319-19920-7_7
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DOI: https://doi.org/10.1007/978-3-319-19920-7_7
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