The stoichiometry and antenna sizes of the two photosystems in two marine green algae, Bryopsis maxima and Ulva pertusa, were investigated to examine whether the photosynthetic apparatus of the algae can be related to the light environment of their natural habitat. Bryopsis maxima and Ulva pertusa had chlorophyll (Chl) a/b ratios of 1.5 and 1.8, respectively, indicating large levels of Chl b, which absorbs blue-green light, relative to Chl a. The level of photosystem (PS) II was equivalent to that of PS I in Bryopsis maxima but lower than that of PS I in Ulva pertusa. Analysis of Q(A) photoreduction and P-700 photo-oxidation with green light revealed that >50% of PS II centres are non-functional in electron transport. Thus, the ratio of the functional PS II to PS I is only 0.46 in Bryopsis maxima and 0.35 in Ulva pertusa. Light-response curves of electron transport also provided evidence that PS I had a larger light-harvesting capacity than did the functional PS II. Thus, there was a large imbalance in the light absorption between the two photosystems, with PS I showing a larger total light-harvesting capacity than PS II. Furthermore, as judged from the measurements of low temperature fluorescence spectra, the light energy absorbed by Chl b was efficiently transferred to PS I in both algae. Based on the above results, it is hypothesized that marine green algae require a higher ATP:NADPH ratio than do terrestrial plants to grow and survive under a coastal environment.

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A water-soluble Chl a/b-protein (CP673) was isolated and purified from Brussels sprouts (Brassica oleracea L. var. gemmifera DC). The protein had a molecular mass of 78 kDa and an isoelectric point of 4.7, consisted of three or four subunits of 22 kDa and was extremely heat-stable. Although CP673 contained about one Chl a per protein, the blue and red absorption bands of Chl a that consisted of three or four Chl a forms with different absorption maxima suggested that there are several different modes or sites of binding for Chl a. Chl a/b ratio of larger than 10 also indicated that Chl b is present only in a small fraction of CP673. The heterogeneity of CP673 in terms of composition and binding of Chl suggests that Chl is not an intrinsic component of the Chl-protein. Homology search showed that the N-terminal amino acid sequence of CP673 is highly homologous with that of a 22 kDa protein that accumulates in water-stressed leaves of two Brassicaceae plants, rapeseed and radish, but not with those of the light-harvesting Chl a/b-proteins of photosynthesis. A possible function of the water-soluble Chl-protein was discussed.

Changes in the Chl a/b ratio, electron transport, electron carriers, and photosystem stoichiometries were examined in rice leaves in the present study. The Chl a/b ratio is known to decrease gradually from the top to the bottom leaves, indicating a increase in the abundance of LHC II relative to the reaction center complexes of the two photosystems. We used juvenile rice canopy and obtained the following results: (1) the photosynthetic activity and Chl content per leaf area decreased from the top to the bottom leaves, the Chl a/b ratio also declined from 3.7 to 3.0; (2) when determined on the basis of Chl content, C-550 and Cyt f content decreased, but there was no loss of P-700, Consequently, the PS II/PS I ratio significantly decreased; (3) on the basis of mmol Chl, the levels of Cyt f dramatically decreased and, therefore, no loss was observed for whole chain electron transport per Cyt f; and (4) the percentage abundance of PS IIa increased, but the rate constants of Q A photoreduction and P-700 photooxidation gradually decreased. From these results, we hypothesize that there is a compensatory relationship between the decline in the Chl a/b ratio and that in the PS II/PS I ratio in the lower leaves in rice seedlings.

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