Hi Dencology. This is a tough one. Let me try to explain.
In order to understand this problem, you need to be aware of the structure of hemoglobing. Hemoglobin, yes an "enzyme" you can say, is not simply composed of a single polypeptide chain. It is as a matter of fact consisting of 4 tetramers bound together. Hemoglobin has a special property - it is an allosteric enzyme. What does that mean? An allosteric enzyme increases its binding affinity towards a molecule as the number of that molecule increase. For example, when a single oxygen molecule binds to the first subunit on hemoglobin, hemoglobin increases its affinity for the 2nd oxygen molecule. Once the 2nd one binds, hemoglobin increases its affinity to the 3rd oxygen molecule, etc...until four oxygen molecules have attached. Great! (This is why carbon monoxide poisoining is so dangerous)
Now lets go to the choices. First, choice E will not work because hemoglobin has a cooperativity of binding. It does not have a 1:1 relationship, but simply increases its affinity as explained above. Linear graph curves are best for enzymes that follow a Michaelis-Menton curve. In other words, their binding affinity is not related to the number of molecules bonded to the enzyme.
Choice A is very poorly written. It is like saying "when you give someone money, you will have more money"...makes no sense. Because hemogloin is an allosteric enzyme, it has a sigmoidal curve, which is shown in the graph. It already is sigmoidal, and rather impossible to change from hyperbolic to sigmoidal. Again hyperbolic graphs follow a Michaelis-Menton curve.
Your understanding for the shift in the curve is correct. Hope this makes more sense.
Thanks.