Abstract
In recent years, significant progress has been made in elucidating the structure of bacteriorhodopsin. However, the molecular mechanism by which vectorial proton motion is enforced remains unknown. Given the advantages of a protonated Schiff base for both photoisomerization and thermal reisomerization of the chromophore, a five-state proton pump can be rationalized in which the switch in the connectivity of the Schiff base between the two sides of the membrane is decoupled from double bond isomerization. This decoupling requires tight control of the Schiff base until it is deprotonated and decisive release after it is deprotonated. NMR evidence has been obtained for both the tight control and the decisive release: strain develops in the chromophore in the first half of the photocycle and disappears after deprotonation. The strain is associated with a strong interaction between the Schiff base and its counterion, an interaction that is broken when the Schiff base deprotonates. Thus the counterion appears to play a critical role in energy transduction, controlling the Schiff base in the first half of the photocycle by ‘electrostatic steering’. NMR also detects other events during the photocycle, but it is argued that these are secondary to the central mechanism.