Each chain is structurally similar to myoglobin Each chain contains a bound heme-Fe2+ Binds a total of 4 oxygen molecules to its four heme groups. Carries O2 from lungs to tissues, increasing the solubility of O2 in blood Spectral changes due to Oxygen binding. ...
These results compare favorably with a value of 1.1 Torr estimated from the work of Rossi-Fanelli and Antonini for human myoglobin. The Hill coefficient, theoretically 1.00 for myoglobin, was experimentally determined to be 0.96 by SVD and 0.95 by curve fitting of the spectral data matrix. 展开...
Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobin The origin of the differences in oxygen binding energy in various haemoglobins and myoglobins has long been debated. Perutz 1 proposed that the haem-coordinated histidine (proximal histidine)...