Structure and bonding Myoglobin

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molecular orbital description of fe-o2 interaction in myoglobin.


myoglobin belongs globin superfamily of proteins, , other globins, consists of 8 alpha helices connected loops. human globin contains 154 amino acids.


myoglobin contains porphyrin ring iron @ center. proximal histidine group (his-93) attached directly iron, , distal histidine group (his-64) hovers near opposite face. distal imidazole not bonded iron available interact substrate o2. interaction encourages binding of o2, not carbon monoxide (co), still binds 240× more o2.


the binding of o2 causes substantial structural change @ fe center, shrinks in radius , moves center of n4 pocket. o2-binding induces spin-pairing : five-coordinate ferrous deoxy form high spin , 6 coordinate oxy form low spin , diamagnetic.








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