Disintegration and reconstitution of Photosystem II reaction center core complex. I. Preparation and characterization of three different types of subcomplex

Reduced content of the quinone acceptor QA in photosystem II complexes isolated from thylakoid membranes after prolonged photoinhibition under anaerobic conditions

“…Quantification of the extracted plastoquinone showed that in control PSI1 core complexes isolated from BBY-membranes kept in the dark there was approximately one plastoquinone molecule per 35 molecules of chlorophyll, which is similar to what has previously been observed in this kind of PSI1 core preparations [22,23]. Photoinhibitory illumination for only 20 min did not give rise to any reduced content of QA in the isolated PSI1 complexes despite a 40% inactivation of the oxygen evolving activity (Fig.…”

L protein, encoded by psbL, restores normal functioning of the primary quinone acceptor, QA, in isolated D1/D2/CP47/Cytb‐559/I photosystem II reaction center core complex

“…The protein compositions in the original, depleted and reconstituted RCs were examined by SDS-PAGE (16-22% polyacrylamide gel with 7.5 M urea) according to Ikeuchi et al [7J PQ-9 and Cytb-559 were analyzed as described in [8] and [9], respectively. The concentration of RC in each RC preparation was determined on the basis of Cytb-559, assuming Cytb-559 per RC = 1 [9].…”

CHLOROPHYLL BINDING PROTEINS WITH ANTENNA FUNCTION IN HIGHER PLANTS and GREEN ALGAE

“…However, only 9-10 Chl a molecules have been quoted per polypeptide in CP43 and CP47 in a recent characterization of PSII subparticles (Akabori et al, 1988).…”