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Dynamic properties of photosystem II membranes at physiological temperatures characterized by elastic incoherent neutron scattering. Increased flexibility associated with the inactivation of the oxygen evolving complex
Nagy, G [Nagy, Gergely (Szilárdtestfizika), szerző] Neutronspektroszkópiai Osztály (SZFKI)
;
Pieper, J
;
Krumova, S B
;
Kovács, L [Kovács, László (molekuláris növén...), szerző] Növénybiológiai Intézet (HRN SZBK)
;
Trapp, M
;
Garab, G [Garab, Győző (Biofizika és növé...), szerző] Növénybiológiai Intézet (HRN SZBK)
;
Peters, J ✉
Angol nyelvű Szakcikk (Folyóiratcikk) Tudományos
Megjelent:
PHOTOSYNTHESIS RESEARCH 0166-8595 1573-5079
111
(1-2)
pp. 113-124
2012
SJR Scopus - Medicine (miscellaneous): Q1
Azonosítók
MTMT: 1999506
DOI:
10.1007/s11120-011-9701-x
WoS:
000302768500013
Scopus:
84858159950
PubMed:
22052408
Google scholar:
13870007293926756131
Szakterületek:
Biológiai tudományok
Egyéb orvostudományok
Klinikai orvostan
Elastic incoherent neutron scattering (EINS), a non-invasive technique which is capable of measuring the mean square displacement of atoms in the sample, has been widely used in biology for exploring the dynamics of proteins and lipid membranes but studies on photosynthetic systems are scarce. In this study we investigated the dynamic characteristics of Photosystem II (PSII) membrane fragments between 280 and 340 K, i.e., in the physiological temperature range and in the range of thermal denaturation of some of the protein complexes. The mean square displacement values revealed the presence of a hydration-sensitive transition in the sample between 310 and 320 K, suggesting that the oxygen evolving complex (OEC) plays an important role in the transition. Indeed, in samples in which the OEC had been removed by TRIS- or heat-treatments (323 and 333 K) no such transition was found. Further support on the main role of OEC in these reorganizations is provided by data obtained from differential scanning calorimetry experiments, showing marked differences between the untreated and TRIS-treated samples. In contrast, circular dichroism spectra exhibited only minor changes in the excitonic interactions below 323 K, showing that the molecular organization of the pigment-protein complexes remains essentially unaffected. Our data, along with earlier incoherent neutron scattering data on PSII membranes at cryogenic temperatures (Pieper et al., Biochemistry 46:11398-11409, 2007), demonstrate that this technique can be applied to characterize the dynamic features of PSII membranes, and can be used to investigate photosynthetic membranes under physiologically relevant experimental conditions. © 2011 Springer Science+Business Media B.V.
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