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NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus . The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesis-specific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under high-light stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term high-light exposure. In contrast, prolonged high-light irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment. NDH-1 is a key component of the cyclic-electron-transfer around photosystem I pathway, an antioxidant mechanism for efficient photosynthesis. Here, authors report a cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus .

The integration of novel components into functional multi-subunit protein complexes is a key evolutionary strategy for enhancing stability, activity, and adaptation to oxidative stress. This is exemplified by the evolution of the conserved photosynthetic NDH-1 (cpNDH-1) complex, though its precise evolutionary history remains unresolved. In this study, we constructed a time-calibrated phylogenetic tree of cyanobacteria to trace the evolutionary trajectory of cpNDH-1. By mapping the orthologous of oxygenic photosynthesis-specific (OPS) subunits onto this tree, we found that the cpNDH-1 complex progressively acquired OPS subunits. Specifically, during the transition from non-photosynthetic to thylakoid-less photosynthetic cyanobacteria, cpNDH-1 incorporated OPS subunits NdhM, NdhN, NdhO, NdhP, and NdhS. Subsequently, NdhL, NdhQ, and NdhV were added as thylakoid-bearing photosynthetic cyanobacteria evolved. Our analysis reveals that the emergence of oxygenic photosynthesis was closely linked with the progressive incorporation of OPS subunits into cpNDH-1. We propose a two-step model for the evolution of these subunits, identifying potential driving factors behind this process. Genome-wide sequence analysis and structural predications further suggest that the OPS cpNDH-1 genes either evolved de novo or arose from modifications of existing genes. Collectively, these findings provide a robust framework for understanding the evolutionary emergence of OPS subunits in cyanobacterial cpNDH-1, underscoring the acquisition of new subunits as a critical adaptation to oxidative environments during the evolution of oxygenic photosynthesis.

Two mutants isolated from a tagging library of Synechocystis sp. strain PCC 6803 were sensitive to high light and had a tag in sll1471 encoding CpcG2, a linker protein for photosystem I (PSI)-specific antenna. Both mutants demonstrated strongly impaired NDH-1-dependent cyclic electron transport. Blue native-polyacrylamide gel electrophoresis followed by immunoblotting and mass spectrometry analyses of the wild type and a mutant containing CpcG2 fused with yellow fluorescent protein-histidine6 indicated the presence of a novel NDH-1L-CpcG2-PSI supercomplex, which was absent in the cpcG2 deletion mutant, the PSI-less mutant, and several other strains deficient in NDH-1L and/or NDH-1M. Coimmunoprecipitation and pull-down analyses on CpcG2-yellow fluorescent protein-histidine6, using antibody against green fluorescent protein and nickel column chromatography, confirmed the association of CpcG2 with the supercomplex. Conversely, the use of antibodies against NdhH or NdhK after blue native-polyacrylamide gel electrophoresis and in coimmunoprecipitation experiments verified the necessity of CpcG2 in stabilizing the supercomplex. Furthermore, deletion of CpcG2 destabilized NDH-1L as well as its degradation product NDH-1M and significantly decreased the number of functional PSI centers, consistent with the involvement of CpcG2 in NDH-1-dependent cyclic electron transport. The CpcG2 deletion, however, had no effect on respiration. Thus, we propose that the formation of an NDH-1L-CpcG2-PSI supercomplex in cyanobacteria facilitates PSI cyclic electron transport via NDH-1L.

Throughout evolution, addition of numerous cyanobacteria-derived subunits to the photosynthetic NDH-1 complex stabilizes the complex and facilitates cyclic electron transfer around photosystem I (PSI CET), a critical antioxidant mechanism for efficient photosynthesis, but its stabilization mechanism remains elusive. Here, a cyanobacteria-derived intermolecular salt bridge is found to form between the two conserved subunits, NdhF1 and NdhD1. Its disruption destabilizes photosynthetic NDH-1 and impairs PSI CET, resulting in the production of more reactive oxygen species under high light conditions. The salt bridge and transmembrane helix 16, both situated at the C-terminus of NdhF1, collaboratively secure the linkage between NdhD1 and NdhB, akin to a cramping mechanism. The linkage is also stabilized by cyanobacteria-derived NdhP and NdhQ subunits, but their stabilization mechanisms are distinctly different. Collectively, to the best of our knowledge, this is the first study to unveil the stabilization mechanism of photosynthetic NDH-1 by incorporating photosynthetic components into its conserved subunits during evolution. A cyanobacteria-derived salt bridge between the conserved NdhF1 and NdhD1 subunits stabilizes the photosynthetic NDH-1 complex, providing the first insight into how the evolutionary integration of photosynthetic components ensures its stability.

NaHSO3 addition greatly increases the yield of H2 photoproduction in a unicellular green alga Chlamydomonas reinhardtii through removing O2 and activating hydrogenase but significantly impairs the activity of PSII, an electron source for H2 photoproduction. Here, a stepwise addition mode of total 13 mM NaHSO3, an optimal concentration for H2 photoproduction of C. reinhardtii identified in a previous one step addition method, significantly improved H2 photoproduction. Such improvement was believed to be the result of increased residual PSII activity in an anaerobic background, but was at least independent of two alternative electron sinks for H2 photoproduction, cyclic electron transport around PSI and CO2 assimilation. Based on the above results, we propose that increased residual PSII activity in an anaerobic environment is an efficient strategy to enhance H2 photoproduction in C. reinhardtii , and the stepwise NaHSO3 addition mode is a case study in the strategy.

The mechanisms of acclimating to a nitrogen-fluctuating environment are necessary for the survival of aquatic cyanobacteria in their natural habitats, but our understanding is still far from complete. Here, the synthesis of phycobiliprotein is confirmed to be much earlier than that of photosystem components during recovery from nitrogen chlorosis and an unknown protein Ssr1698 is discovered to be involved in this synthetic process. The unknown protein is further identified as a c -type heme oxygenase ( c HO) in tetrapyrrole biosynthetic pathway and catalyzes the opening of heme ring to form biliverdin IXα, which is required for phycobilin production and ensuing phycobiliprotein synthesis. In addition, the c HO-dependent phycobiliprotein is found to be vital for the growth of cyanobacterial cells during chlorosis and regreening through its nitrogen-storage and light-harvesting functions, respectively. Collectively, the c HO expressed preferentially during recovery from nitrogen chlorosis is identified in photosynthetic organisms and the dual function of this enzyme-dependent phycobiliprotein is proposed to be an important mechanism for acclimation of aquatic cyanobacteria to a nitrogen-fluctuating environment. Cyanobacterial Ssr1698 is a c-type heme oxygenase (cHO) and is involved in phycobiliprotein (PBP) biosynthesis. This cHO-dependent PBP is vital for adapting to nitrogen fluctuations through its nitrogen-storage and light-harvesting functions.

NaHSO addition greatly increases the yield of H photoproduction in a unicellular green alga through removing O and activating hydrogenase but significantly impairs the activity of PSII, an electron source for H photoproduction. Here, a stepwise addition mode of total 13 mM NaHSO , an optimal concentration for H photoproduction of identified in a previous one step addition method, significantly improved H photoproduction. Such improvement was believed to be the result of increased residual PSII activity in an anaerobic background, but was at least independent of two alternative electron sinks for H photoproduction, cyclic electron transport around PSI and CO assimilation. Based on the above results, we propose that increased residual PSII activity in an anaerobic environment is an efficient strategy to enhance H photoproduction in , and the stepwise NaHSO addition mode is a case study in the strategy.

Prefabricated assembly structures play a pivotal role in modern building construction and underground transit developments, offering benefits such as ease of installation, rapid construction, and environmental sustainability. These prefabricated assembly structures are always symmetric and particularly prevalent in projects like subway station construction, where symmetry prefabricated blocks are commonly used. The hoisting and overturning of these blocks are crucial stages in the construction sequence. Given the substantial weight (tens of tons) and size (several meters) of these prefabricated elements, the materials and structural integrity of the metal components, including bolts and steel rods, must meet strict standards during these phases. To ensure stability during overturning and safety throughout hoisting, this paper utilizes a finite element model to analyze the hoisting and overturning of three prefabricated blocks used in subway station assembly. This paper investigates the mechanical behavior of embedded components, such as lifting lugs, steel liners, and hoisting steel rods, during these processes, analyzing their stress and strain. The selection methods of different steel bars (diameter, hollow, solid, etc.) in the hoisting process were obtained, and the operation speed in the hoisting and overturning process was determined, which guided the selection of the hoisting position when the common overturning action was known. The results offer valuable guidelines for the placement and spacing of lifting lugs, as well as the optimal hoisting speed, thereby informing the selection of embedded lifting lugs and the design of operational protocols in actual assembly construction.