Correction to Identification of Mutational Hot Spots for Substrate Diffusion: Application to Myoglobin

In the course of analyzing our simulation datasets with a new methodology, we came across errors in the calculation of the dissociation rate constants reported in our work.¹ In the original paper these were k₋₁ = 15 μs⁻¹ and k₋₁ = 13.6 μs⁻¹ from the reactive flux and the relaxation methods, respectively. After correcting the error, which primarily involved a unit conversion problem, and reanalyzing the discretized simulation trajectories we recover values of k₋₁ = 179 μs⁻¹ and 144 μs⁻¹. The binding rates remain consistent with our previous analysis (k₊₁ = 647 μM⁻¹s⁻¹ and k₊₁ = 325 μM⁻¹s⁻¹, from the reactive flux and the relaxation methods, respectively). As a result of this correction in the misreported values, the resulting equilibrium constant is K = k₊₁/k₋₁= 3.6 M⁻¹ from the reactive flux method and 2.3 M⁻¹ from the relaxation method. These values of the equilibrium constant are actually in better accord with the experimental value (K =2.2 M⁻¹).² This correction leaves the rest of the results of the paper unchanged.

We would like to acknowledge Manuel Dibak and Dr. Mauricio del Razo (Freie Universitat¨ Berlin) for their help spotting this problem.