Vibrational relaxation as the driving force for wavelength conversion in the peridinin-chlorophyll a-protein
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Abstract We present a computationally derived energy transfer model for the peridinin-chlorophyll a-protein (PCP), which invokes vibrational relaxation in the two lowest singlet excited states rather than internal conversion between them. The model allows an understanding of the photoinduced processes without assuming further electronic states or a dependence of the 2Ag state character on the vibrational sub-state. We report molecular dynamics simulations (CHARMM22 force field) and quantum mechanics/molecular mechanics (QM/MM) calculations on PCP. In the latter, the QM region containing a single peridinin (Per) chromophore or a Per-Chl a (chlorophyll a) pair is treated by density functional theory (DFT, CAM-B3LYP) for geometries and by DFT-based multireference configuration interaction (DFT/MRCI) for excitation energies. The calculations show that Per has a bright, green light absorbing 2Ag state, in addition to the blue light absorbing 1Bu state found in other carotenoids. Both states undergo a strong energy lowering upon relaxation, leading to emission in the red, while absorbing in the blue or green. The orientation of their transition dipole moments indicates that both states are capable of excited-state energy transfer to Chl a, without preference for either 1Bu or 2Ag as donor state. We propose that the commonly postulated partial intramolecular charge transfer (ICT) character of a donating Per state can be assigned to the relaxed 1Bu state, which takes on ICT character. By assuming that both 1Bu and 2Ag are able to donate to the Chl a Q band, one can explain why different chlorophyll species in PCP exhibit different acceptor capabilities.
Götze , J P , Karasulu , B , Patil , M & Thiel , W 2015 , ' Vibrational relaxation as the driving force for wavelength conversion in the peridinin-chlorophyll a-protein ' , Biochimica et Biophysica Acta - Bioenergetics , vol. 1847 , no. 12 , pp. 1509–1517 . https://doi.org/10.1016/j.bbabio.2015.07.011
Biochimica et Biophysica Acta - Bioenergetics
Copyright © 2015 Elsevier Inc. All rights reserved. This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at: https://dx.doi.org/10.1016/j.bbabio.2015.07.011
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