BCHS 3304 Chapter Notes - Chapter 7: Porphyrin, Reperfusion Injury, Cooperative Binding
Document Summary
Chapter 7 textbook notes: oxygen binding to myoglobin and hemoglobin. Myoglobin small intracellular protein in vertebrate muscle: most of its 153 residues are members of 8 helices arranged to form a globular protein with approximate dimension 44x44x25a. 6th ligand to the iron atom: his e7 h-bonds to the o2, 2 hydrophobic side chains on the. Hemoglobin has exact c2 symmetry and pseudo- d2 symmetry: o2 binding alters the structure of the entire hemoglobin tetramer deoxyhemoglobin and oxyhemoglobin. Oxygen binds cooperatively to hemoglobin sigmoidal curve cooperative binding: this permits the blood to deliver much more o2 to the tissues than if hemoglobin had a hyperbolic curve with the same p50. ns. Hill plot: hill equation describes the degree of saturation of hemoglobin as a function of po2, the quantity of n, the hill constant, increases with the degree of cooperativity of a reaction. O2 binding increases the affinity of hemoglobin for further o2 binding.
