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Hæmoglobin and Myoglobin: Cooperativity

  • Engelbert Buxbaum

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.

Keywords

Oxygen Partial Pressure Sickle Cell Oxygen Affinity Oxygen Binding Binding Curve 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Engelbert Buxbaum
    • 1
  1. 1.KevelaerGermany

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