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Tytuł artykułu

Lamellar spacing of photosystem II membrane fragments upon dehydration studied by neutron membrane diffraction

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The effect of dehydration on the lamellar spacing of photosystem II (PS II) membrane fragments from spinach has been investigated using neutron membrane diffraction at room temperature. The diffraction data reveal a major peak at a scattering vector Q of 0.049 Å−1 at a relative humidity (r.h.) of 90% corresponding to a repeat distance D of about 129 Å. Upon dehydration to 44% r.h., this peak shifts to about 0.060 Å−1 corresponding to a distance of 104.7±2.5 Å. Within experimental error, the latter repeat distance remains almost the same at hydration levels below 44% r.h. indicating that most of the hydration water is removed. This result is consistent with the earlier finding that hydration-induced conformational protein motions in PS II membrane fragments are observed above 44% r.h. and correlated with the onset electron transfer in PS II (Pieper et al. 2008, Eur. Biophys. J. 37: 657–663).
Wydawca

Rocznik
Tom
2
Numer
1
Opis fizyczny
Daty
otrzymano
2015-10-06
zaakceptowano
2015-11-03
online
2015-12-31
Twórcy
autor
  • Institute of Physics, University
    of Tartu, Tartu, Estonia
  • Institute of Physical Energetics, Riga, Latvia
autor
  • Helmholtz-Zentrum Berlin für Materialien und Energie
    GmbH, Berlin, Germany
  • Max-Volmer-Laboratories, Technical University
    Berlin, Germany
Bibliografia
  • [1] G. Renger, T. Renger, Photosystem II: The machinery of photosyntheticwater splitting, Photosynth. Res. 98, 2008, 53.[WoS]
  • [2] J. Pieper, G. Renger, Protein dynamics investigated by neutronscattering, Photosynth. Res. 102, 2009, 281.
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  • [4] A. Garbers, J. Kurreck, F. Reifarth, G. Renger, F. Parak, Correlationbetween protein flexibility and electron transfer from Q−·Ato QB in PS II membrane fragments from spinach, Biochemistry37, 1998, 11399.
  • [5] P. Kühn, J. Pieper, O. Kaminskaya, H.-J. Eckert, R. E. Lechner,V. Shuvalov, G. Renger, Reaction pattern of Photosystem II:oxidative water cleavage and protein flexibility, Photosyn. Res.84, 2005, 317.
  • [6] J. Pieper, T. Hauß, A. Buchsteiner, K. Baczynski, K. Adamiak,R.E. Lechner, G. Renger, Temperature- and Hydration-Dependent Protein Dynamics in Photosystem II of Green PlantsStudied by Quasielastic Neutron Scattering, Biochemistry 46,2007, 11398.[WoS]
  • [7] O. Kaminskaya, G. Renger, V. Shuvalov, Effect of dehydrationon light induced reactions in Photosystem II: Photoreactionsof cytochrome b559. Biochemistry 42, 2003, 8119.
  • [8] J. Pieper, T. Hauß, A. Buchsteiner, G. Renger G, The effect ofhydration on protein flexibility in photosystem II of greenplants studied by quasielastic neutron scattering. Eur. Biophys.J. 37, 2008, 657.[WoS]
  • [9] F. Gabel, D. Bicout, U. Lehnert, M. Tehei, M. Weik, G. Zaccai,Protein dynamics studied by neutron scattering, Q. Rev. Biophys.35, 2002, 327.
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  • [11] M. Weik, G. Zaccai, N. A. Dencher, D. Oesterhelt, T. Hauß,Structure and hydration of the m-state of the bacteriorhodopsinmutant D96N studied by neutron diffraction, J.Mol. Biol. 275, 1998, 625.
  • [12] K. H. Tang, R. E. Blankenship, Neutron and light scatteringstudies of light-harvesting photosynthetic antenna complexes,Photosynth Res 111, 2012, 205.[WoS]
  • [13] G. Nagy, G. Garab, J. Pieper, Neutron Scattering in PhotosynthesisResearch, in: Contemporary Problems of Photosynthesis(Editors: S. Allakhverdiev, A. B. Rubin, V. A. Shuvalov)Izhevsk Institute of Computer Science, Izhevsk–Moscow,2014, Vol. 1, p. 69–121.
  • [14] G. Nagy, D. Posselt, L. Kovács, J. K. Holm, M. Szabó, B. Ughy,L. Rosta, J. Peters, P. Timmins, G. Garab, Reversible membranereorganizations during photosynthesis in vivo: revealed bysmall-angle neutron scattering, Biochem. J. 436, 2011, 225.[WoS]
  • [15] B. Daum, D. Nicastro, J. Austin, J. R. McIntosh, W. Kühlbrandt,Arrangement of photosystem II and ATP synthase in chloroplastmembranes of spinach and pea. The Plant Cell 22, 2010,1299.[WoS]
  • [16] J. J. K. Kirkensgaard, J. K. Holm, J. K. Larsen, D. Posselt, Simulationof small-angle X-ray scattering from thylakoid membranes,J. Appl. Crystallogr. 42, 2009, 649.[WoS]
  • [17] A. Zouni, H.-T. Witt, J. Kern, P. Fromme, N. Krauß, W. Saenger, P.Orth, Crystal structure of photosystem II from Synechococcuselongatus at 3.8 Å resolution, Nature 409, 2001, 739.
  • [18] Y. Umena, K. Kawakami, J.-R. Shen, N. Kamiya, Crystal structureof oxygen-evolving photosystem II at a resolution of 1.9A,Nature 473, 2011, 55.
  • [19] Z. Liu, H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An, W.Chang, Crystal structure of spinach major light-harvestingcomplex at 2.72 A resolution, Nature, 428 (6980), 2004, 287.
  • [20] J. Voigt, T. Renger, R. Schödel, T. Schrötter, J. Pieper, H. Redlin,Excitonic effects in the light-harvesting Chl a/b-protein complexof higher plants, Phys Status Solidi B, 194 (1), 1996, 333.
  • [21] J. Pieper, K.-D. Irrgang, M. Rätsep, T. Schrötter, J. Voigt, G.J. Small, G. Renger, Effects of aggregation on trimeric lightharvestingcomplex II of green plants: A hole-burning study, JPhys Chem A 103 (14), 1999, 2422.[Crossref]
  • [22] J. Texeira, M.-C. Bellissent-Funel, S. H. Chen, A. J. Dianoux,Experimental determination of the nature of diffusive motionsof water molecules at low temperature, Phys. Rev. A 31, 1985,1913.
  • [23] J. Pieper, G. Charalambopoulou, T. Steriotis, S. Vasenkov,A. Desmedt, R. E. Lechner, Water Diffusion in Fully HydratedPorcine Stratum Corneum, Chemical Physics 292, 2003, 465.
  • [24] J. Pieper, K.-D. Irrgang, G. Renger, R. E. Lechner, Density ofVibrational States of the Light-Harvesting Complex II of GreenPlants Studied by Inelastic Neutron Scattering, J. Phys. Chem.B 108, 2004, 10556.
  • [25] G. Schiro, Y. Fichou, F.-X. Gallat, K. Wood, F. Gabel, M. Moulinet al., Translational diffusion of hydration water correlateswith functional motions in folded and intrinsically disorderedproteins, Nature Comm. 2015, DOI: 10.1038/ncomms7490[Crossref][WoS]
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_1515_optof-2015-0005
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