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• W2012122513 abstract "The light-driven pump Halorhodopsin (hR) uses the energy stored in an initial meta-stable state (K), in which the bound retinal chromophore has been photoisomerized from all-trans to 13-cis, to drive the translocation of one chloride anion across the membrane. Thus far it was unclear whether retinal twisting or charge separation between the positive Schiff base of the retinal and the chloride anion is the primary mechanism of energy storage. Here, combined quantum mechanical/molecular mechanical (QM/MM) simulations show that the energy is predominantly stored by charge separation. However, a large variability in retinal twisting is observed, thus reconciling the contradictory hypotheses for storage. Surprisingly, the energy stored in the K-state amounts to only one-fifth of the photon energy. We explain why the protein cannot store more: even though this would accelerate chloride pumping, raising the K-state also reduces the relative energy barriers against unproductive decay, in particular via the premature cis to trans back-isomerization. Indeed, the protein has maximized its storage so that the back-isomerization barriers are just high enough (> or =18 kcal/mol) to keep the decay rate (1/100 ms) slower than the remaining photocycle (1/20 ms). This need to stabilize the captured photon-energy until it can be used in subsequent steps is inherent to light-driven proteins." @default.
• W2012122513 created "2016-06-24" @default.
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• W2012122513 date "2009-05-01" @default.
• W2012122513 modified "2023-10-16" @default.
• W2012122513 title "The Mechanism of Photo-energy Storage in the Halorhodopsin Chloride Pump" @default.
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• W2012122513 doi "https://doi.org/10.1074/jbc.m808787200" @default.
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