Abstract
In the light-driven proton pump bacteriorhodopsin, photoisomerization of the all-trans retinal chromophore triggers a photocycle whose net effect is the transfer of one proton from the cytoplasmic to the extracellular side of the membrane. The first proton transfer step, from the retinal Schiff base to Asp85, occurs between the L and M intermediate states. Details of the geometry of the retinal binding region are important for the pathway followed by the proton. Here we report some preliminary results on combined Quantum Mechanical/Molecular Mechanical reaction path calculations for retinal deprotonation and discuss the hydrogen-bonding pattern in the active site.
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