to Table 2. (Reproduced by permission from Nature (Ref. 62). Copyright 2000 Macmillan Magazines Ltd.) Table 2 Thermodynamic and Kinetic Parameters for Redox-Coupled Proton Transfer at A.v. FdI and Mutant Forms, Extracted from Protein Film Voltammetry Experiments

doi:10.1201/9780203908907-77

Chapter

to Table 2. (Reproduced by permission from Nature (Ref. 62). Copyright 2000 Macmillan Magazines Ltd.) Table 2 Thermodynamic and Kinetic Parameters for Redox-Coupled Proton Transfer at A.v. FdI and Mutant Forms, Extracted from Protein Film Voltammetry Experiments

Chapter

ABSTRACT

Interaction between the cluster and the aspartate carboxylate is an important part of the electron-proton coupling mechanism. Once the cluster is protonated, the pK of the D15 carboxylate decreases to a value approaching that observed when the cluster is oxidized (pK1>>pK2~pKox). Simultaneously, the pK of the cluster is sensitive to the protonation state of the aspartate.