Abstract
The 33 kDa protein of Photosystem II has one intrachain disulfide bond. Fluorescence spectroscopy shows that the major groups in the protein that bind to Ca2+ should be the carboxylic side groups of glutamic acid and/or aspartic acid. Fluorescence and Fourier-transform infrared (FTIR) spectroscopic studies indicate that the conformation of the 33 kDa protein is altered upon reduction, while the reduced protein still retains the secondary structure. FTIR spectroscopy also shows that the metal ions induce a relative decrease of unordered structure and β-sheet, and a substantial increase of α-helix in both the intact and the reduced 33 kDa protein. This indicates that the addition of cations results in a much more compact structure and that both the intact and the reduced 33 kDa proteins have the ability to bind calcium. The above results may suggest that the disulfide bridge is not essential for calcium binding.
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Abbreviations
- CD:
-
circular dichroism
- FTIR:
-
Fourier transform infrared
- La:
-
lanthanum
- PS:
-
photosystem
- Tb:
-
terbium
References
Aizawa K and Ohata K (1987) In vitro study of the binding of terbium to tryptophan by 1H-NMR and fluorescence spectroscopy. Biochem Biophys Res Commun 146: 791–796
Beauregard M (1992) Modelling of the Photosystem II 33 kDa protein: Structure, function and possible sulfate-sensitive sites derived from sequence encoded information. Environ Exp Bot 32: 411–429
Coleman WJ and Govindjee (1987) A model for the mechanism of chloride activation of oxygen evolution in Photosystem II. Photosynth Res 13: 199–223
Chou PY and Fasman GD (1978) Prediction of the secondary structure of protein from their amino acid sequence. J Adv Enzym 47: 45–148
Ghanotakis DF and Yocum CF (1990) Photosystem II and the oxygen-evolving complex. Annu Rev Plant Physiol Plant Mol Biol 41: 255–276
Holly S, Laczkó I, Fasman GD and Hollósi M (1993a) Circular dichrosim and Fourier-transform infrared spectroscopic studies on T-cell epitopic peptide fragments of influenza virus hemagglutinin. Biochem Biophys Res Commun 197: 755–762
Holly S, Majer Z, Tóth G K, Váradi G, Rajnavölgyi É, Laczkó I and Hollósi M (1993b) FT-IR spectroscopy indicates that Ca2+-binding to phosphorylated C-terminal fragments of the midsized neurofilament protein submit results in β-sheet formation and β-aggregation Biochem Biophys Res Commun 193: 1247–1254
Horrocks W DeWjr (1982) Lanthanide ion probes of biomolecular structure. In: Eichhorn GL and Marzilla LG (eds) Advances in Inorganic Biochemistry, Vol 4, pp 201–262. Elsevier Science Publishing Company, New York
Jackson M, Haris PI and Chapman D (1991) Fourier transform infrared spectroscopic studies of Ca2+-binding proteins. Biochemistry 30: 9681–9686
Jin YJ, Li WL and Wang QR (1991) Tb(III) as a fluorescence probe for the structure of bovine serum albumin. Biochem Biophys Res Commun 177: 474–479
Kuwabara T and Murata N (1982a) Inactivation of photosynthetic oxygen evolution and concomitant release of three polypeptides in the Photosystem II particles of spinach chloroplasts. Plant Cell Physiol 23: 533–530
Kuwabara T and Murata N (1982b) An improved purification method and a further characterization of the 33 kDa protein of spinach chloroplsts. Biochem Biophys Acta 680: 210–215
Kuwabara T, Murata T, Miyao M and Murata N (1986) Partial degradation of the 18-kDa protein of the photosynthetic oxygen-evolving complex: A study of a binding site. Biochem Biophys Acta 850: 146–150
Lakowicz JR (1983) Protein fluorescence. In: Lakowicz JR (ed) Principles of Fluorescence Spectroscopy, pp 341–348. Plenum Press, New York
Miyao M and Murata N (1984) Role of the 33 kDa protein in preserving Mn in the photosynthetic oxygen-evolution system and its replacement by chloride ions. FEBS Lett 170: 350–354
Oh-oka H, Tanaka S, Wada K, Kuwabara T and Murata N (1986) Complete amino acid sequence of 33 kDa protein isolated from spinach Photosystem II particles. FEBS Lett 197: 63–66
Philibrick JB and Zilinskas BA (1988) Cloning, nucleotide sequence and mutational analysis of the gene encoding the Photosystem II manganese-stabilizing polypeptide of Synechocystis 68093. Mol Gen Genet 212: 418–425
Snyder EE, Buoscio BW and Falke JJ (1990) calcium(II) site specificity. Effect of size and charge on metal ion binding to an EF-hand-like site. Biochemistry 29: 3937–3943
Susi H and Byler DM (1986) Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol 130: 290–311
Tanaka S and Wada K (1988) The status of cysteine residues in the extrinsic 33 kDa protein of spinach Photosystem II complexes. Photosynth Res 17: 255–266
Tanaka S, Kawata Y, Wada K and Hamaguchi K (1989) Extrinsic 33-kilodalton protein of spinach oxygen-evolving complexes: Kinetic studies of folding and disulfide reduction. Biochemistry 28: 7188–7193
Trewhella J, Liddle WK, Heidorn DB and Strynadka N (1989) Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: Effects of Ca2+ and Mg2+ binding. Biochemistry 28: 1294–1301
Wales R, Newman BJ, Pappin D and Gray JC (1989) The extrinsic 33 kDa polypeptide of the oxygen-evolving complex of Photosystem II is a putative calcium-binding protein and is encoded by a multiple-gene family in pea. Plant Mol Biol 12: 439–451
Webber AN and Gray JC (1989) Detection of calcium binding by Photosystem II polypeptides immobilized onto nitrocellulose membrane. FEBS Lett 249: 79–81
Xu Q, Nelson J and Bricker TM (1994) Secondary structure of the 33 kDa extrinsic protein of Photosystem II: A far-UV circular dichrosim. Biochem Biophys Acta 1188: 427–431
Zhang LX and Liang HG (1995) Detection of Ca2+-binding proteins of Photosystem 2 particles by electrophoretic migration combined with terbium fluorescence. Photosynthetica 31: 621–624
Zhang LX, Wang J and Liang HG (1995) Investigation of Ca2+-binding sites on the 33 kDa protein in Photosystem 2 using Tb3+ as a fluorescence probe. Photosynthetica 31: 203–208
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Zhang, LX., Liang, HG., Wang, J. et al. Fluorescence and Fourier-transform infrared spectroscopic studies on the role of disulfide bond in the calcium binding in the 33 kDa protein of Photosystem II. Photosynth Res 48, 379–384 (1996). https://doi.org/10.1007/BF00029470
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DOI: https://doi.org/10.1007/BF00029470