Abstract
The detergent effect on Cytochrome b559 from spinach photosystem II was studied by electron paramagnetic resonance (EPR) spectroscopy in D1-D2-Cyt b559 complex preparations. Various n-dodecyl-ß-D-maltoside concentrations from 0 to 0.2% (w/v) were used to stabilise the D1-D2-Cyt b559 complexes. Low spin heme EPR spectra were obtained but the gz feature positions changed depending on the detergent conditions. Redox potentiometric titrations showed a unique redox potential cytochrome b559 form (E′m = +123-150 mV) in all the D1-D2-Cyt b559 complex preparations indicating that detergent does not affect this property of the protein in those conditions. A similar effect on Cytochrome b559 EPR spectrum was observed in more intact photosystem II preparations independently of their aggregation state. This finding indicates that changes due to detergent could be a common phenomenon in photosystem II complexes. Results are discussed in terms of the environment each detergent provides to the protein.
Similar content being viewed by others
Explore related subjects
Discover the latest articles and news from researchers in related subjects, suggested using machine learning.References
O. Nanba, K. Satoh, Isolation of a photosystem II reaction center consisting of D1 and D2 polypeptides and cytochrome b559, Proc. Natl. Acad. Sci. USA, 1987, 84, 109–112.
X. S. Tang, K. Fushimi, K. Satoh, D1-D2 complex of the photosystem II reaction center from spinach. Isolation and partial characterization, FEBS Lett., 1990, 273, 257–260.
W. R. Widger, W. A. Cramer, M. Hermodson, D. Meyer, M. Gullifor, Purification and partial amino acid sequence of the chloroplast cytochrome b-559, J. Biol. Chem., 1984, 259, 3870–3876.
W. A. Cramer, J. Whitmarsh, Photosynthetic cytochromes, Annu. Rev. Plant Physiol., 1977, 28, 133–172.
J. Whitmarsh, and H. B. Pakrasi, Form and function of cytochrome b559, in Oxygenic Photosysnthesis: The Light Reactions, ed. D. R. Ort and C. F. Yocum, Kluwer Academic Publishers, Dordrecht, The Netherlands. 1996, pp. 249–264.
D. H. Stewart, G. W. Brudvig, Cytochrome b559 of photosystem II, Biochim. Biophys. Acta, 1998, 1367, 63–87.
A. Zouni, H.-T. Witt, J. Kern, P. Fromme, N. Krausse, W. Saenger, P. Orth, Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution, Nature, 2001, 409, 739–743.
P. R. Rich, D. S. Bendall, The redox potentials of the b-type cytochromes of higher plant chloroplasts, Biochim. Biophys. Acta, 1980, 591, 153–161.
J. M. Ortega, M. Hervás, M. Losada, Redox and acid-base characterization of cytochrome b559 in photosystem II particles, Eur. J. Biochem., 1988, 171, 449–455.
O. Kaminskaya, J. Kurreck, K. D. Irrgang, G. Renger, V. A. Shuvalov, Redox and spectral properties of cytochrome b559 in different preparations of photosystem II, Biochemistry, 1999, 38, 16223–16235.
N. Mizusawa, T. Yamashita, M. Miyao, Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions, Biochim. Biophys. Acta, 1999, 1410, 273–286.
M. Roncel, J. M. Ortega, M. Losada, Factors determining the special redox properties of photosynthetic cytochrome b559, Eur. J. Biochem., 2001, 268, 4961–4968.
J. Bergstrom, T. Vanngard, EPR signals and orientation of cytochromes in the spinach chloroplast thylakoid membrane, Biochim. Biophys. Acta, 1982, 682, 452–456.
L. K. Thompson, A.-F. Miller, C. A. Buser, J. C. de Paula, G. W. Brudvig, Characterization of the multiple forms of cytochrome b559 in photosystem II, Biochemistry, 1989, 28, 8048–8056.
C. Berthomieu, A. Boussac, W. Mäntele, J. Breton, E. Nabedryk, Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds, Biochemistry, 1992, 31, 11460–11471.
G. T. Babcock, W. R. Widger, W. A. Cramer, W. A. Oertling, J. G. Metz, Axial ligands of chloroplast cytochrome b559: Identification and requirement for a heme-cross-linked polypeptide structure, Biochemistry, 1985, 24, 3638–3645.
L. I. Krishtalik, G. S Cherepanov, W. A. Cramer, The redox properties of cytochromes b imposed by the membrane electrostatic environment, Biophys. J., 1983, 65, 184–195.
D. A. Berthold, G. T. Babcock, C. F. Yocum, A highly resolved oxygen-evolving photosystem II preparation from spinach thylakoid membranes, FEBS Lett., 1981, 134, 231–234.
G. Montoya, R. Cases, I. Yruela, R. Picorel, Spectroscopic characterization of two forms of the D1-D2-cytochrome b559 complex from sugar beet, Photochem. Photobiol., 1993, 58, 724–729.
I. Yruela, P. J. M. van Kan, M. G. Müller, A. R. Holzwarth, Characterization of a D1-D2-cyt b559 complex containing 4 chlorophyll a/2 pheophytin a isolated with the use of MgSO4, FEBS Lett., 1994, 339, 25–30.
I. Yruela, R. Tomás, M. Alfonso, R. Picorel, Effect of the pH on the absorption spectrum of the isolated D1-D2-cytochrome b559 complex of photosystem II, J. Photochem. Photobiol. B: Biol., 1999, 50, 129–136.
I. Yruela, E. Torrado, M. Roncel, R. Picorel, Light-induced absorption spectra of the D1-D2-cytochrome b559 complex of photosystem II: effect of methyl viologen concentration, Photosynth. Res., 2001, 67, 199–206.
C. Eijckelhoff, J. P. Dekker, A routine to determine the chlorophyll a, pheophytin a and ß-carotene contents of isolated Photosystem II reaction center complexes, Photosynth. Res., 1997, 52, 69–73.
P. J. van Leeuwen, M. C. Nieveen, E. J. van de Meet, J. P. Dekker, H. J. van Gorkom, Rapid and simple isolation of pure photosystem II core and reaction center particles from spinach, Photosynth. Res., 1991, 28, 149–153.
D. Zheleva, B. Hankamer, J. Barber, Heterogeneity and pigment composition of isolated photosystem II reaction centers, Biochemistry, 1996, 35, 15074–15079.
B. Hankamer, J. Nield, D. Zheleva, E. Boekema, S. Jansson, J. Barber, Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo, Eur. J. Biochem., 1997, 243, 422–429.
C. P. S. Taylor, The EPR of low spin heme complexes, Biochim. Biophys. Acta, 1977, 491, 137–149.
V. A. Shuvalov, R. Fiege, U. Schreiber, F. Lendzian, W. Lubitz, EPR study of cytochrome in the D1-D2-Cyt b559 complex, Biochim. Biophys. Acta, 1995, 1228, 175–180.
B. Gall, H. Scheer, Stabilization of photosystem II reaction centers: influence of bile salt detergents and low pH, FEBS Lett., 1998, 431, 161–166.
D. F. Ghanotakis, C. F. Yocum, Purification and properties of an oxygen evolving reaction center complex from photosystem II membranes, FEBS Lett., 1986, 197, 244–248.
R. M. Garavito, S. Ferguson-Miller, Detergents as a tool in membrane biochemistry, J. Biol. Chem., 2001, 276, 32403–32406.
M. le Maire, P. Champeil, J. V. Möller, Interaction of membrane proteins and lipids with solubilizing detergents, Biochim. Biophys. Acta, 2000, 1508, 86–111.
M. Seibert, Biochemical, biophysical and structural characterization of the isolated Photosystem II reaction center complex, in The Photosynthetic Reaction Center, ed. J. Deisenhofer and J. R. Norris, Academic Press, San Diego, CA, 1993, vol. 1, pp. 319–356.
G. Montoya, R. Cases, R. Rodríguez, M. Aured, R. Picorel, Detergent-induced reversible denaturation of the photosystem II reaction center: Implications for pigment-protein interactions, Biochemistry, 1994, 33, 11798–11804.
F. A. Walker, B. H. Huynh, W. R. Scheid, S. R. Osvath, Models of the cytochromes b. Effect of axial ligand plane orientation on the EPR and Mössbauer spectra of low-spin ferrihemes, J. Am. Chem. Soc., 1986, 108, 5288–5297.
F. A. Walker, D. Reis, V. L. Balke, Models of the cytochromes b. EPR studies of low-spin iron(III) tetraphenylporphyrins, J. Am. Chem. Soc., 1984, 106, 6888–6898.
R. Quinn, M. Nappa, J. S. Valentine, New five- and six-coordinate imidazole and imidazolate complexes of ferric tetraphenylporphyrin, J. Am. Chem. Soc., 1982, 104, 2588–2595.
J. C. Salerno, S. Yoshida, T. E. King, Effects of protein-protein and protein-lipid interactions on heme site conformation in the mitochondrial b cytochromes, J. Biol. Chem., 1986, 261, 5480–5486.
B. Lanne, B. G. Malmström, T. Vänngard, The influence of pH on the EPR and redox properties of cytochrome c oxidase in detergent solution and in phospholipid vesicles, Biochim. Biophys. Acta, 1979, 545, 205–214.
M. A. Noordermeer, G. A. Veldink, J. F. G. Vliegenthart, Spectroscopic studies on the active site of hydroperoxide lyase; the influence of detergents on its conformation, FEBS Lett., 2001, 489, 229–232.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Yruela, I., García-Rubio, I., Roncel, M. et al. Detergent effect on Cytochrome bb559 electron paramagnetic resonance signals in the photosystem II reaction centre. Photochem Photobiol Sci 2, 437–442 (2003). https://doi.org/10.1039/b300187c
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1039/b300187c

