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523 Photosystem II: a multisubunit membrane protein that oxidises water James Barber A structure of photosystem II recently determined by X-ray Together, these RC proteins bind all the redox-active crystallography at 3.8 ? resolution complements structural cofactors involved in the energy conversion process and studies using high-resolution electron microscopy and the following sequence of reactions occurs. Firstly, a represents a major step towards understanding how special form of Chla, P680 (the primary electron donor of photosynthetic organisms use light energy to PSII), acts as an exciton trap and is converted to a strong oxidise water. reducing agent after excitation (P680*). Within a few picoseconds, P680* reduces a pheophytin (Pheo) molecule Addresses to form the radical pair state P680?+Pheo?– and, within a Wolfson Laboratories, Department of Biological Sciences, Imperial further few hundred picoseconds, Pheo?– reduces a College of Science, Technology Medicine, London SW7 2AY, UK; plastoquinone molecule bound to the D2 protein (QA) to e-mail: j.barber@ic.ac.uk ?+ – ?+ produce P680 PheoQA . The P680 , which has a very Current Opinion in Structural Biology 2002, 12:523–530 high redox potential (1V), oxidises a tyrosine residue (YZ) ?+ – of the D1 protein (Tyr161) to form YZ P680PheoQA on a 0959-440X/02/$ — see front matter