Abstract
Changes in the protein secondary structure and electron transport activity of the Triton X-100-treated photosystem I (PSI) and photosystem II (PSII) complexes after strong illumination treatment were studied using Fourier transform-infrared (FT-IR) spectroscopy and an oxygen electrode. Short periods of photoinhibitory treatment led to obvious decreases in the rates of PSI-mediated electron transport activity and PSII-mediated oxygen evolution in the native or Triton-treated PSI and PSII complexes. In the native PSI and PSII complexes, the protein secondary structures had little changes after the photoinhibitory treatment. However, in both Triton-treated PSI and PSII complexes, short photoinhibition times caused significant loss of α-helical content and increase of β-sheet structure, similar to the conformational changes in samples of Triton-treated PSI and PSII complexes after long periods of dark incubation. Our results demonstrate that strong-light treatment to the Triton-treated PSI and PSII complexes accelerates destruction of the transmembrane structure of proteins in the two photosynthetic membranes.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
REFERENCES
Ananthapadmanabhan, K. P. (1993). In Interactions of Surfactants with Polymers and Proteins (Goddard, E. D., and Ananthapadmanabhan, K. P., eds.), CRC Press, Boca Raton, Florida, pp. 319–365.
Armbrust, T. S., Chitnis, P. R., and Guikema, J. A. (1996). Plant Physiol. 111, 1307–1312.
Arnon, D. (1949). Plant Physiol. 24, 1–14.
Aro, E. M., Hundal, T., Carlberg, I., and Anderson, B. (1990). Biochim. Biophys.Acta 1019, 269–275.
Aro, E. M., Virgin, I., and Anderson, B. (1993) Biochim.Biophys.Acta 1143, 113–134.
Arrondo, J. L. R., Young, N. M., and Mantsch, H. H. (1988). Biochim. Biophys.Acta 952, 261–268.
Arrondo, J. L. R., Castresana, J., Valpuesta, J. M., and Goni, F. M. (1994). Biochemistry 33, 11650–11655.
Baba, K., Itoh, S., Hastings, G., and Hoshina, S. (1996). Photosyn.Res. 47, 121–130.
Barber, J. and Andersson, B. (1992). Trends Biochem.Sci. 17, 61–66.
Bassi, R. and Simpson, D. (1987). Eur.J.Biochem. 163, 221–230.
Berthold, D. A., Babcock, G. T., and Yocum, C. F. (1981). FEBS Lett. 134, 231–234.
Braun, P., Greenberg, B. M., and Sherz, A. (1990). Biochemistry 29, 10376–10387.
Byler, D. M. and Susi, H. (1986). Biopolymers 25, 469–487.
Dong, A. C., Huang, P., and Caughey, W. S. (1990). Biochemistry 29, 3303–3308.
Gounaris, K., Whitford, D., and Barber, J. (1983). FEBS Lett. 163, 230–234.
He, W. Z., Newell, W. R., Haris, P. I., Chapman, D., and Barber, J. (1991). Biochemistry 30, 4552–4559.
Krauss, N., Schubert, W. D., Klukas, O., Fromme, P., Witt, H. T., and Saenger, W. (1996). Nat.Struct.Biol. 3, 965–973.
Kuwabara, T. and Murata, N. (1982). Plant Cell Physiol. 23, 533–539.
Montoya, G., Cases R., Rodriguez, R., Aured, M., and Picorel, R. (1994). Biochemistry 33, 11798–11804.
Mullet, J. E., Burke, J. J., and Arntzen, C. J. (1980). Plant Physiol. 65, 814–822.
Ono, T., Noguchi, T., and Nakajima, Y. (1995). Biochim.Biophys.Acta 1229, 239–248.
Powies, S. B. (1984). Annu.Rev.Plant Physiol. 35, 15–44.
Ruan, X., Wei, J., Xu, Q., Wang, J. S., Gong, Y. D., Zhang, X. F., Kuang, T. Y., and Zhao, N. M. (2000). J.Mol.Struct. 525, 97–106.
Savitsky, A. and Golay, J. E. (1964). Anal.Chem. 36, 1628–1639.
Shi, H., **ong, L., Yang, K. Y., Tang, C. Q., Kuang, T. Y., and Zhao, N. M. (1998). J.Mol.Struct. 446, 137–147.
Shipton, C. A. and Barber, J. (1991). Proc.Natl.Acad.Sci.USA 88, 6691–6695.
Siegenthaler, P. A., Rawyler, A., and Smutny, J. (1989). Biochim.Biophys. Acta 975, 104–111.
Sonoike, K. (1996). Plant Cell Physiol. 37, 239–247.
Sonoike, K. (1999). J.Photochem.Photobiol.B Biol. 48, 136–141.
Surewitz, W. K. and Mantsch, H. H. (1988). Biochim.Biophys.Acta 952, 115–130.
Tang, D., Jankowiak, R., Seibert, M., and Small, G. J. (1991). Photosyn. Res. 27, 19–29.
Vass, I., Styring, S., Hundal, T., Koivuniemi, A., Aro, E. M., and Andersson, B. (1992). Proc.Natl.Acad.Sci.USA 89, 1408–1412.
Williams, W. (1994). Prog.Lipid Res. 33, 119–127.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ruan, X., Xu, Q., Mao, Hb. et al. Strong-Light Photoinhibition Treatment Accelerates the Changes of Protein Secondary Structures in Triton-Treated Photosystem I and Photosystem II Complexes. J Protein Chem 20, 247–254 (2001). https://doi.org/10.1023/A:1010908210655
Published:
Issue Date:
DOI: https://doi.org/10.1023/A:1010908210655