Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.

ABSTRACT: The role of protein dynamics in enzyme catalysis is one of the most highly debated topics in enzymology. The main controversy centers around what may be defined as functionally significant conformational fluctuations and how, if at all, these fluctuations couple to enzyme catalyzed events. To shed light on this debate, the conformational dynamics along the transition path surmounting the highest free energy barrier have been herein investigated for the rate limiting proton transport event in human carbonic anhydrase (HCA) II. Special attention has been placed on whether the motion of an excess proton is correlated with fluctuations in the surrounding protein and solvent matrix, which may be rare on the picosecond and subpicosecond time scales of molecular motions. It is found that several

SUBMITTER: Taraphder S 

PROVIDER: S-EPMC5003118 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature