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This editorial refers to ‘Significance of myoglobin as an oxygen store and oxygen transporter in the intermittently perfused human heart: a model study’ by V. Endeward et al. , pp. 22–29, this issue. Myoglobin (Mb) belongs to the family of vertebrate oxygen-binding haem proteins and is predominantly expressed in cardiac and red skeletal muscles that rely on aerobic metabolism to perform sustained work.1 Additional members of this protein family are of course haemoglobin, the red dye of blood, and the more recently discovered proteins neuroglobin and cytoglobin. Owing to the notoriously low solubility of oxygen in aqueous solutions, haem proteins such as haemoglobin and Mb substantially enhance the total oxygen content in blood and muscle, respectively, and therefore represent important oxygen stores. Mb is expressed at high concentrations in the heart (∼200 µM), and therefore Mb is thought to buffer short phases of ischaemia by release of oxygen when capillary oxygen supply is limited. Another function of Mb, termed ‘facilitated oxygen diffusion’, postulates that besides a flux of physically dissolved oxygen a flux of Mb-bound oxygen may exist.1 According to this model, oxygen is picked up by Mb at the plasma membrane and is transported to the mitochondria, where it is released and fed into the respiratory chain. In principle, both of these oxygen-related functions of Mb could be relevant because the oxygen partial pressure for half saturation of …

Myoglobin: safeguard of myocardial oxygen supply during systolic compression?