Protein composition and Mn abundance were compared between the two photosystem II (PSII) particle preparations obtained before and after photoactivation of the latent 02-evolving system in intermittently flashed wheat leaves. The following results have been obtained: (a) In the last 5 years, biochemical characterization of the O2-evolving apparatus has advanced dramatically. Initiated by the successful preparation of 0-evolving PSII particles from spinach (3,12,25), intensive studies have been revealing the structural relationships between the PSII reaction center (24, 27) and the 02-evolving apparatus, in particular the roles of the three extrinsic proteins (33, 24, and 16 kD). The 16 and 24 kD proteins are considered to play regulatory roles in 02-evolution by affording high affinity binding for Cl-and Ca2+ (plus Cl-), respectively (1, 2, 9), while the 33 kD protein seems to play a role in stabilizing the Mn atoms in the 02-evolving center (19,20) and thereby enabling them to carry out the linear 4-step oxidation of water (22).We report here some of the changes in biochemical properties ofthe PSII particles that occur when Imfwheat leaves are exposed to continuous light to activate the 02-evolving centers. It was clearly shown that during photoactivation the 16 and 24 kD proteins are integrated into the 02-evolving apparatus, concomitantly with incorporation of 3 Mm atoms into the apparatus, to attain catalytically functional states.