24 February 2009 Anti-correlation of the emission from different red pools in photosystem I
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Electron and energy transfer in proteins are key processes in bioenergetics. Their understanding on a molecular level can serve as an important guideline for the design of nanoscale assemblies. Energy transfer between pigment molecules requires a match between their transition energies for energy emission and absorption. The tuning of these pigment energies in proteins is achieved by pigment-protein interactions. In general, these interactions are regarded as static properties determined by the three-dimensional structure of pigment-protein complexes. Employing single-molecule fluorescence spectroscopy we demonstrate that protein dynamics, even at cryogenic temperatures, significantly influences the transition energy of pigments and, as a consequence, modulates energy transfer pathways. This variability of excitation energy transfer pathways introduced by protein dynamics might be important for the extreme robustness of photosystems.
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M. Brecht, M. Brecht, V. Radics, V. Radics, J. B. Nieder, J. B. Nieder, R. Bittl, R. Bittl, "Anti-correlation of the emission from different red pools in photosystem I", Proc. SPIE 7185, Single Molecule Spectroscopy and Imaging II, 718506 (24 February 2009); doi: 10.1117/12.809303; https://doi.org/10.1117/12.809303

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