Skip to main content
SpringerLink
Log in

Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex

  • Published:
Photosynthetica

Abstract

The protein secondary structure and pigments' microenvironment in photosystem 1 (PS1) complexes were studied in the temperature range of 25–80 °C using Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy, respectively. Quantitative analysis of the component bands of the amide I band (1 700–1 600 cm−1) showed no significant change below 50 °C. However, apparent conformational changes occurred at 60 °C and further continued at 70 and 80 °C accompanied with transitions of secondary structure mainly from α-helix to the β-sheet structures. CD analysis demonstrated that the regular arrangement, viz. protein microenvironment of pigments of PS1 complexes, was destroyed by heat treatment which might come from the changes of protein secondary structure of PS1. The CD signals at 645 nm contributed by chlorophyll (Chl) b of light-harvesting complex 1 (LHC1) were easily destroyed at the beginning of heat treatment (25–60 °C). When temperature reached 70 and 80 °C, the CD signals at 478 nm contributed mainly by Chl b of LHC1 and 498 nm contributed by carotenoids decreased most rapidly, indicating that LHC1 was more sensitive to high temperature than core complexes. In addition, the oxygen uptake rate decreased by 90.81 % at 70 °C and was lost completely at 80 °C showing that heat treatment damaged the regular function of PS1 complexes. This may be attributed to heat-induced changes of pigment microenvironment and protein secondary structure, especially transmembrane α-helix located in PsaA/B of PS1.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

Car:

carotenoid

CD:

circular dichroism

Chl:

chlorophyll

FTIR:

Fourier transform infrared

LHC1:

light-harvesting complex 1

P700:

primary electron donor

PS1:

photosystem 1

RC:

reaction centre

References

  • Armond, P.A., Bjorkman, O., Staehelin, L.A.: Dissociation of supramolecular complexes in chloroplast membranes. A manifestation of heat damage to the photosynthetic apparatus. — Biochim. biophys. Acta 601: 433–442, 1980.

    PubMed  Google Scholar 

  • Arnon, D.I.: Copper enzymes in isolated chloroplasts. Polyphenoxidase in Beta vulgaris. — Plant Physiol. 24: 1–15, 1949.

    Google Scholar 

  • Barber, J., Morris, E., Buchel, C.: Revealing the structure of the photosystem II chlorophyll binding proteins, CP43 and CP47. — Biochim. biophys. Acta 1459: 239–247, 2000.

    Google Scholar 

  • Bassi, R., Silvestri, M., Dainese, P., Moya, I., Giacometti, G.M.: Effects of a non-ionic detergent on the spectral properties and aggregation state of the light-harvesting chlorophyll a/b protein complex (LHCII). — J. Photochem. Photobiol. B 9: 335–354, 1991.

    Article  Google Scholar 

  • Bassi, R., Simpson, D.: Chlorophyll-protein complexes of barley photosystem I. — Eur. J. Biochem. 163: 221–230, 1987.

    Article  PubMed  Google Scholar 

  • Ben-Shem, A., Frolow, F., Nelson, N.: Crystal structure of plant photosystem I. — Nature 426: 630–635, 2003.

    Article  PubMed  Google Scholar 

  • Berry, J., Bjorkman, O.: Photosynthetic response and adaption to temperature in higher plants. — Annu. Rev. Plant Physiol. 31: 491–543, 1980.

    Article  Google Scholar 

  • Carpentier, R., Larue, B., Leblanc, R.M.: Photoacoustic spectroscopy of Anacystis nidulans. III. Detection of photosynthetic activities. — Arch. Biochem. Biophys. 338: 534–543, 1984.

    Article  Google Scholar 

  • Chitinis, P.R.: Photosystem I. — Plant Physiol. 111: 661–669, 1996.

    Article  PubMed  Google Scholar 

  • Chitinis, P.R.: Photosystem I: function and physiology. — Annu. Rev. Plant Physiol. Plant mol. Biol. 52: 593–626, 2001.

    Article  PubMed  Google Scholar 

  • Chitnis, P.R., Xu, Q., Chitnis, V.P., Nechushtai, R.: Function and organization of Photosystem I polypeptides. — Photosynth. Res. 44: 23–40, 1995.

    Article  Google Scholar 

  • De Las Rivas, J., Barber, J.: Structure and thermal stability of photosystem II reaction centres studied by infrared spectroscopy. — Biochemistry 36: 8897–8903, 1997.

    Article  PubMed  Google Scholar 

  • Fromme, P., Jordan, P., Krauß, N.: Structure of photosystem I. — Biochim. biophys. Acta 1507: 5–31, 2001.

    PubMed  Google Scholar 

  • Fromme, P., Schubert, W.D., Krauß, N.: Structure of Photosystem I: Suggestions on the docking sites for plastocyanin, ferredoxin and the coordination of P700. — Biochim. biophys. Acta 1187: 99–105, 1994.

    PubMed  Google Scholar 

  • Golbeck, J.H.: Structure and function of photosystem I. — Annu. Rev. Plant Physiol. Plant mol. Biol. 43: 293–324, 1992.

    Article  Google Scholar 

  • Haworth, P., Watson, J.L., Arntzen, C.J.: The detection, isolation and characterization of a light-harvesting complex which is specifically associated with photosystem I. — Biochim. biophys. Acta 724: 151, 1983.

    Google Scholar 

  • He, W.-Z., Newell, W.R., Haris, P.I., Chapman, D., Barber, J.: Protein secondary structure of the isolated photosystem II reaction centre and conformational changes studied by Fourier transformation infrared spectroscopy. — Biochemistry 30: 4552–4559, 1991.

    Article  PubMed  Google Scholar 

  • Hu, Z.H., Xu, Y.N., Jiang, G.Z, Kuang, T.Y.: Degradation and inactivation of photosystem I complexes during linear heating. — Plant Sci. 166: 1177–1183, 2004.

    Article  Google Scholar 

  • Ilik, P., Kouril, R., Fiala, J., Naus, J., Vacha, F.: Spectral characterization of chlorophyll fluorescence in barley leaves during linear heating analysis of high-temperature fluorescence rise around 60 °C. — J. Photochem. Photobiol. B 59: 103–114, 2000.

    Article  PubMed  Google Scholar 

  • Jordan, P., Fromme, P., Klukas, O., Witt, H.T., Saenger, W., Krauß, N.: Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. — Nature 411: 909–917, 2001.

    Article  PubMed  Google Scholar 

  • Klukas, O., Schubert, W.D., Jordan, P., Krauß, N., Fromme, P., Witt, H.T., Saenger, W.: Localization of two phylloquinones, QK and QK′, in an improved electron density map of photosystem I at 4-Å resolution. — J. biol. Chem. 274: 7361–7367, 1999a.

    Article  PubMed  Google Scholar 

  • Klukas, O., Schubert, W.D., Jordan, P., Krauß, N., Fromme, P., Witt, H.T., Saenger, W.: Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and PsaE. — J. biol. Chem. 274: 7351–7360, 1999b.

    Article  PubMed  Google Scholar 

  • Krimm, S., Bandekar, J.: Vibrational spectroscopy and conformation of peptides, polypeptides and proteins. — Adv. Protein Chem. 38: 181–364, 1986.

    PubMed  Google Scholar 

  • Lam, E., Ortiz, W., Malkin, R.: Chlorophyll a/b proteins of photosystem I. — FEBS Lett. 168: 10–14, 1984.

    Article  Google Scholar 

  • Morgan, R., Ivanov, A.G., Williams, J., Khan, M., Huner, N.P.A.: Differential thermal effects on the energy distribution between photosystem II and photosystem I in thylakoid membranes of a psychrophilic and a mesophilic alga. — Biochim. biophys. Acta 1561: 251–265, 2002.

    PubMed  Google Scholar 

  • Mullet, J.E., Burke, J.J., Arntzen, C.J.: Chlorophyll proteins of photosystem I. — Plant Physiol. 65: 814–822, 1980.

    Google Scholar 

  • Nechushtai, R., Eden, A., Cohen, Y., Klein, J.: Introduction to photosystem I: reaction centre function, composition and structure. — In: Ort, D.R., Yocum, C.F. (ed.): Oxygenic Photosynthesis: The Light Reactions. Pp. 289–311. Kluwer Academic Publ., Dordrecht — Boston — London 1996.

    Google Scholar 

  • Ruan, X., Wei, J., Xu, Q., Wang, J.S., Gong, Y.D., Zhang, X.F., Kuang, T.Y., Zhao, N.M.: Comparison of the effects of Triton X-100 treatment on the protein secondary structure of photosystem I and photosystem II studied by FT-IR spectroscopy. — J. mol. Struct. 525: 97–106, 20000.

    Article  Google Scholar 

  • Ruban, A.V., Calkoen, F., Kwa, S.L.S., Grondelle, R.V., Horton, P., Dekker, J.P.: Characterization of LHCII in the aggregated state by linear and circular dichroism spectroscopy. — Biochim. biophys. Acta 1321: 61–70, 1997.

    Google Scholar 

  • Scheller, H.V., Jensen, P.E., Haldrup, A., Lunde, C., Knoetzel, J.: Role of subunits in eukaryotic photosystem I. — Biochim. biophys. Acta 1507: 41–60, 2001.

    PubMed  Google Scholar 

  • Schubert, W.D., Klukas, O., Saenger, W., Witt, H.T., Fromme, P., Krauß, N.: A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of photosystem I. — J. mol. Biol. 280: 297–314, 1988.

    Article  Google Scholar 

  • Shi, H., Xiong, L., Yang, K.Y., Tang, C.Q., Kuang, T.Y., Zhao, N.M.: Protein secondary structure and conformational changes of photosystem II during heat denaturation studied by Fourier transform infrared spectroscopy. — J. mol. Struct. 446: 137–147, 1998.

    Article  Google Scholar 

  • Somsen, O.J., Grondelle, R.V., Amerongen, H.V.: Spectral broadening of interacting pigments: polarized absorption by photosynthetic proteins. — Biophys. J. 71: 1934–1951, 1996.

    PubMed  Google Scholar 

  • Surewicz, W.K., Mantsch, H.H.: New insight into protein secondary structure from resolution-enhanced infrared spectra. — Biochim. biophys. Acta 952: 115–130, 1988.

    PubMed  Google Scholar 

  • Takeuchi, T.S., Thornber, J.P.: Heat-induced alterations in thylakoid membrane protein composition in barley. — Aust. J. Plant Physiol. 21: 759–770, 1994.

    Google Scholar 

  • Wang, M., Zhong, Z.P., Wang, K.B., Li, L.B., Kuang, T.Y.: Isolation of chlorophyll protein complexes from the thylakoid membrane in Nostoc flagelliforme and their spectroscopic characterization. — Acta bot. sin. 42: 684–688, 2000.

    Google Scholar 

  • Wei, J., Yu, H., Li, L.B., Kuang, T.Y., Wang, J.S., Gong, Y.D., Zhao, N.M.: The photodamage process of pigments and proteins of PS I complexes from Spinacia oleracea L. — Chin. Sci. Bull. 46: 1812–1816, 2001.

    Google Scholar 

  • Zhang, H., Yamamoto, Y., Ishikawa, Y., Carpentier, R.: Characterization of the secondary structure and thermostability of the extrinsic 16 kilodalton protein of spinach photosystem II by Fourier transform infrared spectroscopy. — J. mol. Struct. 513: 127–132, 1999.

    Article  Google Scholar 

  • Zhong, Z.P., Wu, Y.H., Xu, J., Feng, L.J., Shi, D.J.: Differentiation of hormogonia and photosynthetic characterization of Nostoc flagelliforme. — Acta bot. sin. 42: 570–575, 2000.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Key Laboratory of Photosynthesis and Environmental Molecular Physiology, Institute of Botany, the Chinese Academy of Sciences, Beijing, 100093, China

    Z.-H. Hu, Y.-N. Xu & T.-Y. Kuang

  2. State Key Laboratory of Biomembrane and Membrane Biotechnology, Department of Biological Science and Biotechnology, Tsinghua University, Beijing, 100084, China

    Y.-D. Gong

Authors
  1. Z.-H. Hu
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Y.-N. Xu
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Y.-D. Gong
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. T.-Y. Kuang
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hu, ZH., Xu, YN., Gong, YD. et al. Effects of heat treatment on the protein secondary structure and pigment microenvironment in photosystem 1 complex. Photosynthetica 43, 529–534 (2005). https://doi.org/10.1007/s11099-005-0085-z

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11099-005-0085-z

Additional key words

Search

Navigation