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The effects of light-induced reduction of the photosystem II reaction center

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Abstract

Accumulation of reduced pheophytin a (Pheo-D1) in photosystem II reaction center (PSII RC) under illumination at low redox potential is accompanied by changes in absorbance and circular dichroism spectra. The temperature dependences of these spectral changes have the potential to distinguish between changes caused by the excitonic interaction and temperature-dependent processes. We observed a conformational change in the PSII RC protein part and changes in the spatial positions of the PSII RC pigments of the active D1 branch upon reduction of Pheo-D1 only in the case of high temperature (298 K) dynamics. The resulting absorption difference spectra of PSII RC models equilibrated at temperatures of 77 K and 298 K were highly consistent with our previous experiments in which light-induced bleaching of the PSII RC absorbance spectrum was observable only at 298 K. These results support our previous hypothesis that Pheo-D1 does not interact excitonically with the other chlorins of the PSII RC, since the reduced form of Pheo-D1 causes absorption spectra bleaching only due to temperature-dependent processes.

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Notes

  1. Multiple time steps of 1 fs for intramolecular and 2 fs for intermolecular forces was found the most appropriate. A cutoff of 0.8 nm was used for Lennard-Jones and electrostatic interactions. To treat long-range electrostatic interactions outside the cutoff region, the particle mesh Ewald (PME) method [53] with a grid spacing < 0.1nm, 4th order B-splines and a tolerance of 10−4 for the direct space sum were used. The temperature was adjusted by Berendsen thermostat [54] based on the time-averaged temperature.

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Acknowledgments

Support from the Institutional Research Concept of the Academy of Science of the Czech Republic (AVOZ60870520 and AV0Z50510513) and from the Ministry of Education of the Czech Republic (LC 06010 and MSM6007665808) and the Grant Agency of the Czech Republic (203/08/0114) is gratefully acknowledged.

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Authors and Affiliations

  1. Institute of Physical Biology, University of South Bohemia, Zamek 136, 37333, Nove Hrady, Czech Republic

    Peter Palencar, Tatyana Prudnikova, Frantisek Vacha & Michal Kuty

  2. Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic, Zamek 136, 37333, Nove Hrady, Czech Republic

    Peter Palencar & Michal Kuty

  3. Biological Centre, Academy of Sciences of the Czech Republic, Branisovska 31, 370 05, Ceske Budejovice, Czech Republic

    Frantisek Vacha

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  1. Peter Palencar
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Correspondence to Michal Kuty.

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Supplementary Fig. 1

Conformational analysis of Neutral-MD (solid lines polynomically fitting raw data represented by squares) and Pheo–MD simulations (dashed lines polynomically fitting raw data represented by triangles) at 298 K performed on selected spherical protein layers of Eq-PSII RC model. (a1) Root mean square deviations of alpha carbons (Cα RMSD) of the whole D1 protein subunit, and Cα RMSD of D1 spherical layers that differ by increasing distance from Pheo-D1 head group: (a2) the first layer within 0.00-0.23 nm from Pheo-D1, (a3) the second layer within 0.23-0.5 nm, and finally (a4) the third layer within 0.50-0.70 nm). (b1) Cα RMSD of of the whole D2 protein subunit, and Cα RMSD of protein layers of D2 that differ by increasing distance from Pheo-D1 head group, layers (b2), (b3) and (b4) are defined analogous to Supplementary Fig. 1a (PDF 2.09 MB)

Supplementary Fig. 2

Conformational analysis (RMSD plots) of Pheo–MD simulations on NA (solid lines polynomically fitting raw data represented by squares) and NC atoms (dashed lines polynomically fitting raw data represented by triangles) of PSII RC chlorins, under (a) 298 K and (b) 77 K. Both of the plots consist of two columns. The first column exhibits the results from a conformational analysis of the PSII RC pigments from the active D1 branch and the second column from the inactive D2 branch, respectively (PDF 1.20 MB)

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Palencar, P., Prudnikova, T., Vacha, F. et al. The effects of light-induced reduction of the photosystem II reaction center. J Mol Model 15, 923–933 (2009). https://doi.org/10.1007/s00894-008-0448-z

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