Proton transport in carbonic anhydrase: Insights from molecular simulation.

摘要: This article reviews the insights gained from molecular simulations of human carbonic anhydrase II (HCA II) utilizing non-reactive and reactive force fields. The with a field explore protein transfer transport via Grotthuss shuttling, while probe larger conformational dynamics that underpin various contributions to rate-limiting proton event. Specific attention is given orientational stability His64 group characteristics active site water cluster, in an effort determine both their impact on maximal catalytic rate. explicit events are described by multistate empirical valence bond (MS-EVB) method, as alternative pathways for excess charge defect enter/leave site. simulation results interpreted light experimental wild-type enzyme site-specific mutations HCA order better elucidate key factors contribute its exceptional efficiency.