Answer to Question #138765 in Physical Chemistry for Yuki

Question

ADP was far in excess of the enzyme concentration for all of the measurements.

The relaxation effect was assumed to arise from a conformational change in the enzymeADP complex.

E+ADP to (EADP)1, equilibrium constant K1

Then, (EADP)1 to (EADP)2, equilibrium constant K2

(EADP)2 to (EADP)1, equilibrium constant K-2

which follows the rapid equilibrium of enzyme-ADP complex formation.

The first step is considered to be in equilibrium on the time scale of the conformational change. Thus, write down the expression for the equilibrium constant K1, rearrange to get [E] alone on the left hand side and differentiate with respect to EADP1 to arrive at an expression relating ΔE to Δ(EADP)1. Because ADP was in excess, you can assume that [ADP] is a constant.

Answer 1

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