Oxygen-binding cooperativity: what are the typical Hill coefficients? In protein-ligand binding, estimate the Hill coefficient (nH) values most commonly observed for myoglobin versus hemoglobin, respectively (physiology/biochemistry context).

Introduction / Context:
Hemoglobin and myoglobin are classic models for cooperative versus noncooperative ligand binding. The Hill coefficient nH is an empirical measure of cooperativity. Values near 1 indicate noncooperative binding, whereas values greater than 1 indicate positive cooperativity. Understanding these values is essential for interpreting oxygen-transport physiology and enzyme allostery.

Given Data / Assumptions:

• Myoglobin contains one heme and binds one O2 molecule.
• Hemoglobin is a tetramer that can bind up to four O2 molecules.
• We use typical textbook, physiological conditions to quote representative nH values.

Concept / Approach:
Because myoglobin has a single binding site, it cannot exhibit classical cooperativity; thus its Hill coefficient is approximately 1. Hemoglobin displays positive cooperativity arising from T (tense) to R (relaxed) quaternary transitions upon O2 binding, producing a sigmoidal O2 saturation curve and an apparent Hill coefficient around 2.8 to 3.0 under physiological conditions.

Step-by-Step Solution:
Recognize nH ≈ 1 indicates noncooperative behavior, the case for single-site myoglobin.Recognize nH > 1 indicates positive cooperativity; hemoglobin typically shows nH about 2.8.Match options to these values to select the correct pair.

Verification / Alternative check:
Plotting log(Y/(1 − Y)) versus log(pO2) gives the Hill plot slope near half-saturation. Myoglobin’s slope is approximately 1; hemoglobin’s slope is near 2.8 under standard conditions.

Why Other Options Are Wrong:
Pairs such as 2.8 and 1.0 invert the correct assignment; very large values like 4.5 are inconsistent with physiological hemoglobin; values below 1 for myoglobin or above 3.5 for hemoglobin are not typical.

Common Pitfalls:
Confusing the maximal possible slope with the number of binding sites; nH does not have to equal the number of sites, it reflects the steepness of the binding curve near mid-saturation.

Final Answer:
1.0 and 2.8.