Question

explain why H+ is considered to be a negative heterotropic allosteric effector in hemoglobin and the describe the mechanism by which it is able to affect the O2 affinity

Answer 1

Allosteric means it change the shape and activates the proton.

It binds with another molecule and ability to react the molecule.

H⁺ is heterotopic allosteric protein. Its not the enzyme substrate.

It inhibitor of the enzyme. It decreases the oxygen ability in heamoglobin.

So H⁺ is considered as negative allosteric effector in heamoglobin.

O₂ is the homotopic allosteric proton. It activates the enzyme.

Heamoglobin has the binding capacity of oxygen.

Oxygen increase the total blood capacity.

Heamoglobin binds the four oxygen molecules.

The oxygen is able to oxidise Fe⁺² to Fe⁺³.