Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation

Zouni A, Kern J, Frank J, Hellweg T, Behlke J, Saenger W, Irrgang KD (2005)
Biochemistry 44(11): 4572-4581.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The oxygen-evolving photosystern 11 core complexes (PS11cc) from the thermophilic cyanobacteriurn Thermosynechococcus elongatus (PSIIccTe) and the higher plant Spinacia oleracea (PSIIccSo) have been isolated from the thylakoid membrane by solubilization with n-dodecyl-beta-D-maltoside, purified and characterized by gel permeation chromatography (GPC), dynamic light scattering (DLS), and analytical ultracentrifugation (AUC. DLS suggests that PSIIcc from both organisms exists as a monomer in dilute solution and aggregates with increasing protein concentration. In contrast to DLS, GPC and AUC showed that PS11cc of both organisms occur as monomers and dimers, and it became clear from our studies that calibration of GPC columns with soluble proteins leads to wrong estimates of the molecular masses of membrane proteins. At a PSIIcc protein concentration of 0.2 mg/mL, molar masses, M, of 756 +/- 18 kDa and 710 +/- 15 kDa for dimeric PSIIccTe and PSIIccSo, respectively, were determined by analytical ultracentrifugation. At very low protein concentrations, at or below 0.05 mg/mL, the dimeric form of PSIIccTe partially dissociates (20-30%) to form monomers. On the basis of these studies 3-dimensional crystals of PSIIccTe were obtained that contain dimers in the asymmetric unit [Zouni, A. et a]. (2001) Nature 409, 739-743]. Using synchrotron radiation the crystals diffract to a resolution of 3.8 angstrom, which has been improved recently to 3.2 angstrom [Biesiadka, J., et al. (2004) Phys. Chem. Chem. Phys. 6, 4733-4736].
Erscheinungsjahr
Zeitschriftentitel
Biochemistry
Band
44
Zeitschriftennummer
11
Seite
4572-4581
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eISSN
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Zouni A, Kern J, Frank J, et al. Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry. 2005;44(11):4572-4581.
Zouni, A., Kern, J., Frank, J., Hellweg, T., Behlke, J., Saenger, W., & Irrgang, K. D. (2005). Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry, 44(11), 4572-4581. doi:10.1021/bi047685q
Zouni, A., Kern, J., Frank, J., Hellweg, T., Behlke, J., Saenger, W., and Irrgang, K. D. (2005). Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry 44, 4572-4581.
Zouni, A., et al., 2005. Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry, 44(11), p 4572-4581.
A. Zouni, et al., “Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation”, Biochemistry, vol. 44, 2005, pp. 4572-4581.
Zouni, A., Kern, J., Frank, J., Hellweg, T., Behlke, J., Saenger, W., Irrgang, K.D.: Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry. 44, 4572-4581 (2005).
Zouni, A, Kern, J, Frank, J, Hellweg, Thomas, Behlke, J, Saenger, W, and Irrgang, KD. “Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation”. Biochemistry 44.11 (2005): 4572-4581.

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Daten bereitgestellt von Europe PubMed Central.

Improvements in serial femtosecond crystallography of photosystem II by optimizing crystal uniformity using microseeding procedures.
Ibrahim M, Chatterjee R, Hellmich J, Tran R, Bommer M, Yachandra VK, Yano J, Kern J, Zouni A., Struct Dyn 2(4), 2015
PMID: 26726311
Variation of exciton-vibrational coupling in photosystem II core complexes from Thermosynechococcus elongatus as revealed by single-molecule spectroscopy.
Skandary S, Hussels M, Konrad A, Renger T, Müh F, Bommer M, Zouni A, Meixner AJ, Brecht M., J Phys Chem B 119(11), 2015
PMID: 25708355
Two types of fucoxanthin-chlorophyll-binding proteins I tightly bound to the photosystem I core complex in marine centric diatoms.
Ikeda Y, Yamagishi A, Komura M, Suzuki T, Dohmae N, Shibata Y, Itoh S, Koike H, Satoh K., Biochim Biophys Acta 1827(4), 2013
PMID: 23416844
The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity.
Wellert S, Tiersch B, Koetz J, Richardt A, Lapp A, Holderer O, Gäb J, Blum MM, Schulreich C, Stehle R, Hellweg T., Eur Biophys J 40(6), 2011
PMID: 21416312
Recent progress in the crystallographic studies of photosystem II.
Guskov A, Gabdulkhakov A, Broser M, Glöckner C, Hellmich J, Kern J, Frank J, Müh F, Saenger W, Zouni A., Chemphyschem 11(6), 2010
PMID: 20352642
Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6-a resolution.
Broser M, Gabdulkhakov A, Kern J, Guskov A, Müh F, Saenger W, Zouni A., J Biol Chem 285(34), 2010
PMID: 20558739
Probing the accessibility of the Mn(4)Ca cluster in photosystem II: channels calculation, noble gas derivatization, and cocrystallization with DMSO.
Gabdulkhakov A, Guskov A, Broser M, Kern J, Müh F, Saenger W, Zouni A., Structure 17(9), 2009
PMID: 19748343
Structure of the Mn4-Ca cluster as derived from X-ray diffraction.
Kern J, Biesiadka J, Loll B, Saenger W, Zouni A., Photosynth Res 92(3), 2007
PMID: 17492491
A comparative approach towards thylakoid membrane proteome analysis of unicellular green alga Scenedesmus obliquus.
Kantzilakis K, Aivaliotis M, Kotakis C, Krasanakis F, Rizos AK, Kotzabasis K, Tsiotis G., Biochim Biophys Acta 1768(9), 2007
PMID: 17574204

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