TIME-RESOLVED DYNAMICS OF PROTON-TRANSFER IN PROTEINOUS SYSTEMS

The dynamics of proton dissociation from an acidic moiety and its subs equent dispersion in the bulk is regulated by the physical chemical pr operties of the solvent. The solvent has to provide a potential well t o accommodate the discharged proton, screen it from the negative charg e of the conjugated base, and provide an efficient mode for the diffus ion of the proton to the bulk. On measuring the dynamics of proton dis sociation in the time-resolved domain, the kinetic analysis of the rea ction can quantitate the properties of the immediate environment. In t his review we implement the kinetic analysis for evaluating the proper ties of small cavities in proteins and the diffusion of protons within narrow channels. On the basis of this analysis,we discuss how the clu stering of proton-binding sites on a surface can endow the surface wit h enhanced capacity to attract protons and to funnel them toward a spe cific site.