Temperature-dependent vibrational and conformational dynamics of photosystem II membrane fragments from spinach investigated by elastic and inelastic neutron scattering

Vibrational and conformational protein dynamics of photosystem II (PS II) membrane fragments from spinach were investigated by elastic and inelastic incoherent neutron scattering (EINS and IINS). As to the EINS experiments, the average atomic mean square displacement values of PS II membrane fragments hydrated at a relative humidity of 57% exhibit a dynamical transition at ~ 230 K. In contrast, the dynamical transition was absent at a relative humidity of 44%. These findings are in agreement with previous studies which reported a “freezing” of protein mobility due to dehydration (Pieper et al. (2008) Eur. Biophys. J. 37: 657–663) and its correlation with an inhibition of electron transfer from QA− to QB (Kaminskaya et al. (2003) Biochemistry 42, 8119–8132). IINS spectra of a sample hydrated at a relative humidity of 57% show a distinct Boson peak at ~ 7.5 meV at 20 K, which shifts towards lower energy values upon temperature increase to 250 K. This unexpected effect is interpreted in terms of a “softening” of the protein matrix along with the onset of conformational protein dynamics as revealed by the EINS experiments. Information on the density of vibrational states of pigment–protein complexes is important for a realistic calculation of excitation energy transfer kinetics and spectral lineshapes and is often routinely obtained by optical line-narrowing spectroscopy at liquid helium temperature. The data presented here demonstrate that IINS is a valuable experimental tool in determining the density of vibrational states not only at cryogenic, but also at nearly physiological temperatures up to 250 K. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial.

► Direct investigation of photosystem II protein dynamics by neutron scattering.
► Vibrational density of states at elevated and nearly physiological temperatures.
► Strong coupling between protein dynamics and function in photosystem II.