Abstract
Degradation of the reaction center-binding protein D1 of Photosystem II (PS II) during photoinhibition is dependent on the action of active oxygen species and/or D1-specific proteases. Protein conformational changes may be involved in the process of D1 degradation. In the present study, we determined the effect of H2O2 on spinach PS II-enriched membranes and core complexes with respect to electron transport, Mn content and protein secondary structural changes as measured by Fourier transform infrared (FTIR) spectroscopy. H2O2 is effective in removing catalytic Mn in PS II, especially in PS II core complexes depleted of OEC18 and OEC24, impairing the donor-side. By quantitative analysis of the amide I band (1600 – 1700 cm-1) with both aqueous and dehydrated PS II samples, we found that no significant secondary structural changes are associated with H2O2 treatment in the dark, even though there is some cleavage of the D1 protein by H2O2 treatment as determined by Western analysis with specific antibodies. In contrast, a large decrease in the α-helices in the PS II core occurs, with or without H2O2 treatment, after 20 min strong illumination and there is more extensive degradation of the D1 protein. Our results suggest that high light enhances the cleavage of the D1 protein which is reflected in the large protein secondary structural changes in PS II detected by FTIR measurements.
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Zhang, H., Yamamoto, Y., Ishikawa, Y. et al. A Fourier transform infrared spectroscopic study of the effects of hydrogen peroxide and high light on protein conformations of Photosystem II. Photosynthesis Research 52, 215–223 (1997). https://doi.org/10.1023/A:1005805510602
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DOI: https://doi.org/10.1023/A:1005805510602