The world's crop productivity is stagnating whereas population growth, rising affluence, and mandates for biofuels put increasing demands on agriculture. Meanwhile, demand for increasing cropland competes with equally crucial global sustainability and environmental protection needs. Addressing this looming agricultural crisis will be one of our greatest scientific challenges in the coming decades, and success will require substantial improvements at many levels. We assert that increasing the efficiency and productivity of photosynthesis in crop plants will be essential if this grand challenge is to be met. Here, we explore an array of prospective redesigns of plant systems at various scales, all aimed at increasing crop yields through improved photosynthetic efficiency and performance. Prospects range from straightforward alterations, already supported by preliminary evidence of feasibility, to substantial redesigns that are currently only conceptual, but that may be enabled by new developments in synthetic biology. Although some proposed redesigns are certain to face obstacles that will require alternate routes, the efforts should lead to new discoveries and technical advances with important impacts on the global problem of crop productivity and bioenergy production.light capture/conversion | carbon capture/conversion | smart canopy | enabling plant biotechnology tools | sustainable crop production Increasing demands for global food production over the next several decades portend a huge burden on the world's shrinking farmlands. Increasing global affluence, population growth, and demands for a bioeconomy (including livestock feed, bioenergy, chemical feedstocks, and biopharmaceuticals) will all require increased agricultural productivity, perhaps by as much as 60-120% over 2005 levels (e.g., refs. 1 and 2), putting increased productivity on a collision course with environmental and sustainability goals (3). The 45 y from 1960 to 2005 saw global food production grow ∼160%, mostly (135%) by improved production on
Site-directed mutations were introduced to replace D1-His198 and D2-His197 of the D1 and D2 polypeptides, respectively, of the photosystem II (PSII) reaction center of Synechocystis PCC 6803. These residues coordinate chlorophylls P A and P B which are homologous to the special pair Bchlorophylls of the bacterial reaction centers that are coordinated respectively by histidines L-173 and M-200 (202). P A and P B together serve as the primary electron donor, P, in purple bacterial reaction centers. In PS II, the site-directed mutations at D1 His198 affect the P + -P-absorbance difference spectrum. The bleaching maximum in the Soret region (in WT at 433 nm) is blue-shifted by as much as 3 nm. In the D1 His198Gln mutant, a similar displacement to the blue is observed for the bleaching maximum in the Q y region (672.5 nm in WT at 80 K), whereas features attributed to a band shift centered at 681 nm are not altered. In the Y Z •-Y Z -difference spectrum, the band shift of a reaction center chlorophyll centered in WT at 433-434 nm is shifted by 2-3 nm to the blue in the D1-His198Gln mutant. The D1-His198Gln mutation has little effect on the optical difference spectrum, 3 P-1 P, of the reaction center triplet formed by P + Pheo -charge recombination (bleaching at 681-684 nm), measured at 5-80 K, but becomes visible as a pronounced shoulder at 669 nm at temperatures g150 K. Measurements of the kinetics of oxidized donor-Q A -charge recombination and of the reduction of P + by redox active tyrosine, Y Z , indicate that the reduction potential of the redox couple P + /P can be appreciably modulated both positively and negatively by ligand replacement at D1-198 but somewhat less so at D2-197. On the basis of these observations and others in the literature, we propose that the monomeric accessory chlorophyll, B A , is a long-wavelength trap located at 684 nm at 5 K. B A * initiates primary charge separation at low temperature, a function that is increasingly shared with P A * in an activated process as the temperature rises. Charge separation from B A * would be potentially very fast and form P A + B A -and/or B A + Pheo -as observed in bacterial reaction centers upon direct excitation of B A ) Proc. Natl. Acad Sci. 96, 2054-2059. The cation, generated upon primary charge separation in PSII, is stabilized at all temperatures primarily on P A , the absorbance spectrum of which is displaced to the blue by the mutations. In WT, the cation is proposed to be shared to a minor extent (∼20%) with P B , the contribution of which can be modulated up or down by mutation. The band shift at 681 nm, observed in the P + -P difference spectrum, is attributed to an electrochromic effect of P A + on neighboring B A . Because of its low-energy singlet and therefore triplet state, the reaction center triplet state is stabilized on B A at e80 K but can be shared with P A at >80 K in a thermally activated process.
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