Dynamically controlled protein tunneling paths in photosynthetic reaction centers.
Marcus theory has explained how thermal nuclear motions modulate the energy gap between donor and acceptor sites in protein electron transfer reactions. Thermal motions, however, may also modulate electron tunneling between these reactions. Here we identify a new mechanism of nuclear dynamics amplification that plays a central role when interference among the dominant tunneling pathway tubes is destructive. In these cases, tunneling takes place in protein conformations far from equilibrium that minimize destructive interference. As an example, we demonstrate how this dynamical amplification mechanism affects certain reaction rates in the photosynthetic reaction center and therefore may be critical for biological function.
Balabin
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IA
Department of Physics, University of California at San Diego, La Jolla, CA 92093-0319, USA.
Onuchic
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D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D003624:Darkness; D004583:Electrons; D006860:Hydrogen Bonding; D008027:Light; D010674:Pheophytins / Q000737:chemistry / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011809:Quinones / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
D010674:Pheophytins; D045322:Photosynthetic Reaction Center Complex Proteins; D011809:Quinones; C006678:bacteriopheophytin