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We previously reported that Asp631 decreased the redox potential (Em) for heme 9 by 136 mV [1,362 mV according to Breuer et al. (1)] in native MtrF, whereas Asp631 protonation (corresponding to Asn631 mutation) did not significantly affect Em for heme 9, because deprotonation of other residues compensated for the Em shift (2). Breuer et al. (3) cannot observe the corresponding effect, since they fixed the protonation states of titratable residues (1). According to Breuer et al. (1), residues make unusually large contributions to Em; for example, Asp228 decreases Em for heme 2 by −2,280 mV [−61 mV in our calculations (2)]. In their letter, Breuer et al. (3) state that “it is only meaningful to compare the sign but not the magnitude of the single-residue contributions”; however, in their original report, they focus on not only the sign but also the magnitude of the single-residue …

Reply to Breuer et al.: Molecular dynamics simulations do not provide functionally relevant values of redox potential in MtrF