Myoglobin oxygen affinity

Synthetic models of myoglobin and hemoglobin are complex molecules that mimic the stereochemical properties of the protein active center [24] and have oxygen affinities similar to those measured for the protein [25-27]. The first heme model that reversibly binds oxygen (i.e. the picket-fence-oxygen complex Fe(TpivPP)(l,2-Melm)(02), shown in Fig. 3.3) was obtained in the early nine-teen-seventies by Collman and coworkers (TpivPP = tetrapivalami-nophenyl porphyrin 2-meIm = 2-methylimidazole) [18]. Research on synthetic models of the protein has led to a deeper understand-... 

As n > 1, there is positive cooperativity, but not to the same extent as in hemoglobin. As P50 — 4.6, which is between that of hemoglobin and myoglobin, the new hemoglobin has a high oxygen affinity. 

Hayashi T, Dejima H, Matsuo T et al (2002) Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity. J Am Chem Soc 124 11226-11227... 

Fig. 5.7 Comparison of Oxygen Affinity Curve for Hemoglobin vs. Myoglobin...

---