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Net photosynthetic CO 2 assimilation rate ( A n ) decreases at leaf temperatures above a relatively mild optimum ( T opt ) in most higher plants. This decline is often attributed to reduced CO 2 conductance, increased CO 2 loss from photorespiration and respiration, reduced chloroplast electron transport rate ( J ), or deactivation of Ribulose-1,5-bisphosphate Carboxylase Oxygenase (Rubisco). However, it is unclear which of these factors can best predict species independent declines in A n at high temperature. We show that independent of species, and on a global scale, the observed decline in A n with rising temperatures can be effectively accounted for by Rubisco deactivation and declines in J . Our finding that A n declines with Rubisco deactivation and J supports a coordinated down-regulation of Rubisco and chloroplast electron transport rates to heat stress. We provide a model that, in the absence of CO 2 supply limitations, can predict the response of photosynthesis to short-term increases in leaf temperature. Photosynthesis declines at mild temperatures in terrestrial plants. Here, the authors use published data to show that decline in photosynthetic CO 2 assimilation rate with rising temperatures can be accounted for by Rubisco deactivation and declines in chloroplast electron transport rate.

In some of our most useful crops (such as rice and wheat), photosynthesis produces toxic by-products that reduce its efficiency. Photorespiration deals with these by-products, converting them into metabolically useful components, but at the cost of energy lost. South et al. constructed a metabolic pathway in transgenic tobacco plants that more efficiently recaptures the unproductive by-products of photosynthesis with less energy lost (see the Perspective by Eisenhut and Weber). In field trials, these transgenic tobacco plants were ∼40% more productive than wild-type tobacco plants. Science , this issue p. eaat9077 ; see also p. 32 Tobacco plants carrying engineered glycolate metabolic pathways showed as much as 40% greater productivity than wild-type plants in field trials. Photorespiration is required in C 3 plants to metabolize toxic glycolate formed when ribulose-1,5-bisphosphate carboxylase-oxygenase oxygenates rather than carboxylates ribulose-1,5-bisphosphate. Depending on growing temperatures, photorespiration can reduce yields by 20 to 50% in C 3 crops. Inspired by earlier work, we installed into tobacco chloroplasts synthetic glycolate metabolic pathways that are thought to be more efficient than the native pathway. Flux through the synthetic pathways was maximized by inhibiting glycolate export from the chloroplast. The synthetic pathways tested improved photosynthetic quantum yield by 20%. Numerous homozygous transgenic lines increased biomass productivity between 19 and 37% in replicated field trials. These results show that engineering alternative glycolate metabolic pathways into crop chloroplasts while inhibiting glycolate export into the native pathway can drive increases in C 3 crop yield under agricultural field conditions.

Cyanobacteria play a significant role in the global carbon cycle. In Synechococcuselongatus, the carbon-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is concentrated into polyhedral, proteinaceous compartments called carboxysomes. Using live cell fluorescence microscopy, we show that carboxysomes are first detected as small seeds of RuBisCO that colocalize with existing carboxysomes. These seeds contain little or no shell protein, but increase in RuBisCO content over several hours, during which time they are exposed to the solvent. The maturing seed is then enclosed by shell proteins, a rapid process that seals RuBisCO from the cytosol to establish a distinct, solvent-protected microenvironment that is oxidizing relative to the cytosol. These closure events can be spatially and temporally coincident with the appearance of a nascent daughter RuBisCO seed. Carboxysomes assemble in a stepwise fashion, inside-to-outside, revealing that cargo is the principle organizer of this compartment's biogenesis. Our observations of the spatial relationship of seeds to previously formed carboxysomes lead us to propose a model for carboxysome replication via sequential fission, polymerization, and encapsulation of their internal cargo.

The CO 2 concentration at ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is crucial to improve photosynthetic efficiency for biomass yield. However, how to concentrate and transport atmospheric CO 2 towards the Rubisco carboxylation is a big challenge. Herein, we report the self-assembly of metal-organic frameworks (MOFs) on the surface of the green alga Chlorella pyrenoidosa that can greatly enhance the photosynthetic carbon fixation. The chemical CO 2 concentrating approach improves the apparent photo conversion efficiency to about 1.9 folds, which is up to 9.8% in ambient air from an intrinsic 5.1%. We find that the efficient carbon fixation lies in the conversion of the captured CO 2 to the transportable HCO 3 − species at bio-organic interface. This work demonstrates a chemical approach of concentrating atmospheric CO 2 for enhancing biomass yield of photosynthesis. Concentrating CO 2 around Rubisco is critical to improve photosynthetic efficiency for biomass yield. Here, the authors report the self-assembly of metal-organic frameworks (MOFs) on the surface of green alga Chlorella pyrenoidosa to enhance the photosynthetic carbon fixation.

Plants invest a considerable amount of leaf nitrogen in the photosynthetic enzyme ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO), forming a strong coupling of nitrogen and photosynthetic capacity. Variability in the nitrogen-photosynthesis relationship indicates different nitrogen use strategies of plants (i.e., the fraction nitrogen allocated to RuBisCO; fLNR), however, the reason for this remains unclear as widely different nitrogen use strategies are adopted in photosynthesis models. Here, we use a comprehensive database of in situ observations, a remote sensing product of leaf chlorophyll and ancillary climate and soil data, to examine the global distribution in fLNR using a random forest model. We find global fLNR is 18.2 ± 6.2%, with its variation largely driven by negative dependence on leaf mass per area and positive dependence on leaf phosphorus. Some climate and soil factors (i.e., light, atmospheric dryness, soil pH, and sand) have considerable positive influences on fLNR regionally. This study provides insight into the nitrogen-photosynthesis relationship of plants globally and an improved understanding of the global distribution of photosynthetic potential. The fraction of leaf nitrogen allocated to RuBisCO indicates differing nitrogen use strategies of plants and varies considerably. Here the authors show that this variation is largely driven by leaf thickness and phosphorus content with light intensity, atmospheric dryness and soil pH also having considerable influence.

Wheat is the second most important direct source of food calories in the world. After considerable improvement during the Green Revolution, increase in genetic yield potential appears to have stalled. Improvement of photosynthetic efficiency now appears a major opportunity in addressing the sustainable yield increases needed to meet future food demand. Effort, however, has focused on increasing efficiency under steady-state conditions. In the field, the light environment at the level of individual leaves is constantly changing. The speed of adjustment of photosynthetic efficiency can have a profound effect on crop carbon gain and yield. Flag leaves of wheat are the major photosynthetic organs supplying the grain of wheat, and will be intermittently shaded throughout a typical day. Here, the speed of adjustment to a shade to sun transition in these leaves was analysed. On transfer to sun conditions, the leaf required about 15 min to regain maximum photosynthetic efficiency. In vivo analysis based on the responses of leaf CO2 assimilation (A) to intercellular CO2 concentration (ci) implied that the major limitation throughout this induction was activation of the primary carboxylase of C3 photosynthesis, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). This was followed in importance by stomata, which accounted for about 20% of the limitation. Except during the first few seconds, photosynthetic electron transport and regeneration of the CO2 acceptor molecule, ribulose-1,5-bisphosphate (RubP), did not affect the speed of induction. The measured kinetics of Rubisco activation in the sun and de-activation in the shade were predicted from the measurements. These were combined with a canopy ray tracing model that predicted intermittent shading of flag leaves over the course of a June day. This indicated that the slow adjustment in shade to sun transitions could cost 21% of potential assimilation. This article is part of the themed issue ‘Enhancing photosynthesis in crop plants: targets for improvement’.

Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO) is the carbon-fixing enzyme present in most photosynthetic organisms, converting CO 2 into organic matter. Globally, photosynthetic efficiency in terrestrial plants has become increasingly challenged in recent decades due to a rapid increase in atmospheric CO 2 and associated changes toward warmer and dryer environments. Well adapted for these new climatic conditions, the C 4 photosynthetic pathway utilizes carbon concentrating mechanisms to increase CO 2 concentrations surrounding RuBisCO, suppressing photorespiration from the oxygenase catalyzed reaction with O 2 . The energy efficiency of C 3 photosynthesis, from which the C 4 pathway evolved, is thought to rely critically on an uninterrupted supply of chloroplast CO 2 . Part of the homeostatic mechanism that maintains this constancy of supply involves the CO 2 produced as a byproduct of photorespiration in a negative feedback loop. Analyzing the database of RuBisCO kinetic parameters, we suggest that in genera ( Flaveria and Panicum ) for which both C 3 and C 4 examples are available, the C 4 pathway evolved only from C 3 ancestors possessing much lower than the average carboxylase specificity relative to that of the oxygenase reaction ( S C/O = S C / S O ), and hence, the higher CO 2 levels required for development of the photorespiratory CO 2 pump (C 2 photosynthesis) essential in the initial stages of C 4 evolution, while in the later stage (final optimization phase in the Flaveria model) increased CO 2 turnover may have occurred, which would have been supported by the higher CO 2 levels. Otherwise, C 4 RuBisCO kinetic traits remain little changed from the ancestral C 3 species. At the opposite end of the spectrum, C 3 plants (from Limonium ) with higher than average S C/O , which may be associated with the ability of increased CO 2 , relative to O 2 , affinity to offset reduced photorespiration and chloroplast CO 2 levels, can tolerate high stress environments. It is suggested that, instead of inherently constrained by its kinetic mechanism, RuBisCO possesses the extensive kinetic plasticity necessary for adaptation to changes in photorespiration that occur in the homeostatic regulation of CO 2 supply under a broad range of abiotic environmental conditions.

Plants depend on the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) for CO₂ fixation. However, especially in C3 plants, photosynthetic yield is reduced by formation of 2-phosphoglycolate, a toxic oxygenation product of Rubisco, which needs to be recycled in a high-flux–demanding metabolic process called photorespiration. Canonical photorespiration dissipates energy and causes carbon and nitrogen losses. Reducing photorespiration through carbon-concentrating mechanisms, such as C4 photosynthesis, or bypassing photorespiration through metabolic engineering is expected to improve plant growth and yield. The β-hydroxyaspartate cycle (BHAC) is a recently described microbial pathway that converts glyoxylate, a metabolite of plant photorespiration, into oxaloacetate in a highly efficient carbon-, nitrogen-, and energy-conserving manner. Here, we engineered a functional BHAC in plant peroxisomes to create a photorespiratory bypass that is independent of 3-phosphoglycerate regeneration or decarboxylation of photorespiratory precursors. While efficient oxaloacetate conversion in Arabidopsis thaliana still masks the full potential of the BHAC, nitrogen conservation and accumulation of signature C4 metabolites demonstrate the proof of principle, opening the door to engineering a photorespiration-dependent synthetic carbon–concentrating mechanism in C3 plants.

Aims Plant invasion can alter the soil microbial community and carbon cycling in terrestrial ecosystems; however, shifts in soil autotrophic bacterial communities and their driving environmental factors after plant invasion remain largely unknown. This study examined the relationship between Moso bamboo (Phyllostachys pubscens) invasion into broadleaf forests and autotrophic bacterial community composition-function at two field sites. Methods The abundance and composition of autotrophic bacteria were characterized by real-time PCR, terminal restriction fragment length polymorphism, and clone library based on the cbbL gene that encodes ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO). Results On average, the cbbL gene abundance was 89% higher and RubisCO enzyme activity 110% higher in the bamboo forest than in the broadleaf forests across the two field sites. The cbbL gene abundance was positively correlated with the RubisCO enzyme activity. The cbbL-containing communities were dominated by the order Rhizobiales, and their composition differed between the forest types and between the two sites, with the effect of site location being greater. Soil readily-oxidizable carbon concentration was a critical factor determining the site location effect on the diversity and activity of the cbbL-containing community. Conclusion Greater abundance and activity of autotrophic bacteria were associated with bamboo invasion into broadleaf forests, implying that such invasions are expected to increase the CO2 fixation potential.

Cells use compartmentalization of enzymes as a strategy to regulate metabolic pathways and increase their efficiency 1 . The α- and β-carboxysomes of cyanobacteria contain ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)—a complex of eight large (RbcL) and eight small (RbcS) subunits—and carbonic anhydrase 2 – 4 . As HCO 3 − can diffuse through the proteinaceous carboxysome shell but CO 2 cannot 5 , carbonic anhydrase generates high concentrations of CO 2 for carbon fixation by Rubisco 6 . The shell also prevents access to reducing agents, generating an oxidizing environment 7 – 9 . The formation of β-carboxysomes involves the aggregation of Rubisco by the protein CcmM 10 , which exists in two forms: full-length CcmM (M58 in Synechococcus elongatus PCC7942), which contains a carbonic anhydrase-like domain 8 followed by three Rubisco small subunit-like (SSUL) modules connected by flexible linkers; and M35, which lacks the carbonic anhydrase-like domain 11 . It has long been speculated that the SSUL modules interact with Rubisco by replacing RbcS 2 – 4 . Here we have reconstituted the Rubisco–CcmM complex and solved its structure. Contrary to expectation, the SSUL modules do not replace RbcS, but bind close to the equatorial region of Rubisco between RbcL dimers, linking Rubisco molecules and inducing phase separation into a liquid-like matrix. Disulfide bond formation in SSUL increases the network flexibility and is required for carboxysome function in vivo. Notably, the formation of the liquid-like condensate of Rubisco is mediated by dynamic interactions with the SSUL domains, rather than by low-complexity sequences, which typically mediate liquid–liquid phase separation in eukaryotes 12 , 13 . Indeed, within the pyrenoids of eukaryotic algae, the functional homologues of carboxysomes, Rubisco adopts a liquid-like state by interacting with the intrinsically disordered protein EPYC1 14 . Understanding carboxysome biogenesis will be important for efforts to engineer CO 2 -concentrating mechanisms in plants 15 – 19 . The structure of a Rubisco–CcmM complex sheds light on the formation of carboxysomes in cyanobacteria.