Myoglobin oxygenation curves

Fig. 4. Oxygenation curves for myoglobin and hemoglobin. The average number of oxygen molecules bound per protein molecule, n, is plotted vs. the partial pressure of O2. For hemoglobin the oxygenation curve is given at three different partial pressures of carbon dioxide...

Myoglobin saturation curve. The saturation of myoglobin is shown as a function of oxygen concentration. 

Fig. 13. Typical oxygen equilibrium curves for haemoglobin (curve a) and myoglobin (curve b) curve c indicates a myoglobin-type (i.e., a non-cooperative oxygenation curve) with the same percentage saturation as haemoglobin at venous oxygen partial pressure.

FIGURE 9.18 The variation of the extent of saturation of myoglobin (Mb) and hemoglobin (Hbl with the partial pressure of oxygen. The different shapes of the curves account for the different biological functions of the two proteins. 

THE OXYGEN DISSOCIATION CURVES FOR MYOGLOBIN HEMOGLOBIN SUIT THEIR PHYSIOLOGIC ROLES... 

The qualitative relationship between the oxygen binding curves for hemoglobin and myoglobin. 

Figure 13.5 (a) The structure of sperm whale myoglobin. (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.) (b) The oxygen-binding curves of myoglobin and haemoglobin. (Reprinted with permission from Collman et al., 2004. Copyright (2004) American Chemical Society.)... 

Hyperbolic shape of the enzyme kinetics curve Most enzymes show Michaelis-Menten kinetics (see p. 58), in which the plot of initial reaction velocity, v0, against substrate concentration [S], is hyperbolic (similar in shape to that of the oxygen-dissociation curve of myoglobin, see p. 29). In contrast, allosteric enzymes frequently show a sigmoidal curve (see p. 62) that is similar in shape to the oxygen-dissociation curve of hemoglobin (see p. 29). 

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