BCH210H1 Chapter Notes - Chapter 9: Carbamate, Reaction Coordinate, Myoglobin

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Conclusion: the lower the ph the less the affinity binding for o2. Bohr effect: the effect of h+ on o2 binding was discovered by christian bohr, binding of protons diminishes oxygen binding, binding of oxygen diminishes proton binding, important physiological significance. Co2 also promotes the dissociation of o2 from hemoglobin: most of the co2 in the tissues are transported back to the mother through the bicarbonate ions (hco3. Review: hemoglobin: 2,3 bpg, allosteric regulator of hb, stabilizes the t-state, o2 stabilizes the r-state. [h+]: stabilizes the t-state as the concentration of h+ increases, shifts o2 binding curve to the right; bohr effect, co2. Stabilizing either states (r or t) are due to conformation changes of hemoglobin: Nucleophilic substitution: enzymes are going to have key residues (2-6) in their active site, at least one of them is going to partake in a nucleophilic attack, when an enzyme has a specific residue.