Dynamic protein conformations preferentially drive energy transfer along the active chain of the photosystem II reaction centre

Lu Zhang, Daniel-Adriano Silva, Houdao Zhang, Alexander Yue, YiJing Yan () and Xuhui Huang ()
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Lu Zhang: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology
Daniel-Adriano Silva: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology
Houdao Zhang: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology
Alexander Yue: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology
YiJing Yan: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology
Xuhui Huang: Institute for Advance Study and School of Science, Hong Kong University of Science and Technology

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract One longstanding puzzle concerning photosystem II, a core component of photosynthesis, is that only one of the two symmetric branches in its reaction centre is active in electron transfer. To investigate the effect of the photosystem II environment on the preferential selection of the energy transfer pathway (a prerequisite for electron transfer), we have constructed an exciton model via extensive molecular dynamics simulations and quantum mechanics/molecular mechanics calculations based on a recent X-ray structure. Our results suggest that it is essential to take into account an ensemble of protein conformations to accurately compute the site energies. We identify the cofactor CLA606 of active chain as the most probable site for the energy excitation. We further pinpoint a number of charged protein residues that collectively lower the CLA606 site energy. Our work provides insights into the understanding of molecular mechanisms of the core machinery of the green-plant photosynthesis.

Date: 2014
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DOI: 10.1038/ncomms5170

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