Exploring Electron Transfer-Induced Conformational Changes in NRH:quinone Oxidoreductase.

Abstract

NRH:quinone oxidoreductase is a flavoenzyme that catalyzes the one-step reduction of quinones to hydroquinones using its cofactor, FAD. The enzyme kinetics goes through a "ping-pong" mechanism, in which changes in the flavin redox state control substrate binding and release. In this study, we are studying the slower dynamics of the subunit interface (surrounding the active site) using Normal Mode Analysis and exploring its relationship with the faster local motions.