Energy-structure correlation in metalloporphyrins and the control of oxygen binding by hemoglobin.
The contribution of the porphyrin skeleton to the potential energy surface metalloporphyrins is calculated by the semiempirical method of quantum mechanical extension of the consistent force field to eta electron molecules. This calculation makes it possible to correlate the observed structure of metalloporphyrins with the strain energy of the porphyrin skeleton. It is found that the out-of-plane metal displacement in pentacoordinate heme systems is due to both the restricted size of the porphyrin hole and the "1-3" steric interaction between the axial ligand and the heme nitrogens. The main components of the active site of hemoglobin are simulated by a histidine-heme-oxygen system. The energy surface of this system provides a quantitative explanation for the control of ligand binding by hemoglobin. It is shown that the heme acts as a diaphragm, designed to provide simultaneous binding to the histidine and the sixth ligand under the steric requirements of the 1-3 interactions. The dependence of the hemoglobin potential surface on the distance between the proximal histidine and the heme plane is evaluated for the R and T states, using the calculated heme potential and the observed energy of heme-heme interaction.
D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006418:Heme / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D008961:Models, Structural; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000378:metabolism*; D011166:Porphyrins / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D008024:Ligands; D010108:Oxyhemoglobins; D011166:Porphyrins; D006418:Heme; D010100:Oxygen
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