Section 4.13: Oxygen Binding
- The binding of oxygen to myoglobin and hemoglobin occurs at the heme group that is noncovalently attached
to the peptide chain
- The heme group contains a porphoryin ring with a ferrous iron atom bound at the center in the reduced
(2+) state. When oxygen binds, the iron is partially oxidized and moves up into the plane of the ring. This partial
oxidation allows for the reversible binding of oxygen, and is accompanied by conformational changes in the protein
structure through movements of two histidine residues