MOLECULAR MECHANISM OF LIGHT-INDUCED PROTON TRANSPORT IN BACTERIORHODOPSIN

A microscopic model of the bacteriorhodopsin (BR) function based on re cent data on an active site structure and the change in intramolecular electrostatic interactions is proposed. Proton dynamic transformation s in an active site caused by a the light-induced charge separation in a chromophore are analyzed. The kinetics of the proton motion along th e outlet channel (H-bonded chain) is considered in the framework of th e small polaron concept. A mechanism of Schiff base reprotonation and recovery of the initial state of BR is discussed.