Photosystem II (PSII) is the pigment-protein complex which converts sunlight energy into chemical energy by catalysing the process of light-driven oxidation of water into reducing equivalents in the form of protons and electrons. Three-dimensional structures from x-ray crystallography have been used extensively to model these processes. However, the crystal structures are not necessarily identical to those of the solubilised complexes. Here we compared picosecond fluorescence of solubilised and crystallised PSII core particles isolated from the thermophilic cyanobacterium Thermosynechococcus elongatus. The fluorescence of the crystals is sensitive to the presence of artificial electron acceptors (K3Fe(CN)(3)) and electron transport inhibitors (DCMU). In PSII with reaction centres in the open state, the picosecond fluorescence of PSII crystals and solubilised PSII is indistinguishable. Additionally we compared picosecond fluorescence of native PSII with PSII in which Ca-2 in the oxygen evolving complex (OEC) is biosynthetically replaced by Sr2+. With the Sr2+ replaced OEC the average fluorescence decay slows down slightly (81 ps to 85 ps), and reaction centres are less readily closed, indicating that both energy transfer/trapping and electron transfer are affected by the replacement. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.
|Number of pages||6|
|Journal||Biochimica et Biophysica Acta (BBA) - Bioenergetics|
|Publication status||Published - 2014|