Abstract
Nonadiabatic ONIOM(CASSCF:AMBER) and CASSCF simulations elucidated different photodynamics of an all-trans retinal protonated Schiff base (RPSB) in bacteriorhodopsin and methanol as well as without an environment. The bR protein matrix holds RPSB tight via specific interactions and promotes bond-specific (along the C13═C14 bond), unidirectional, and ultrafast photoisomerization with a high quantum yield. In contrast, in methanol and for the twisted bare RPSB, photoisomerization is not bond-specific (mainly along the C11═C12 bond), is nonunidirectional, and is ineffective. Therefore, bR efficiently "catalyzes" photoisomerization and stores enough energy to promote the subsequent proton pumping and protein conformational changes.
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