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Photosystem II (PSII) enables global-scale, light-driven water oxidation. Genetic manipulation of PSII from the mesophilic cyanobacterium sp. PCC 6803 has provided insights into the mechanism of water oxidation; however, the lack of a high-resolution structure of oxygen-evolving PSII from this organism has limited the interpretation of biophysical data to models based on structures of thermophilic cyanobacterial PSII. Here, we report the cryo-electron microscopy structure of PSII from sp. PCC 6803 at 1.93-Å resolution. A number of differences are observed relative to thermophilic PSII structures, including the following: the extrinsic subunit PsbQ is maintained, the C terminus of the D1 subunit is flexible, some waters near the active site are partially occupied, and differences in the PsbV subunit block the Large (O1) water channel. These features strongly influence the structural picture of PSII, especially as it pertains to the mechanism of water oxidation.
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http://dx.doi.org/10.1073/pnas.2116765118 | DOI Listing |
ISME J
September 2025
Department of Ecology, Environment and Plant Sciences, Stockholm University, Svante Arrhenius väg 20A, SE-106 91 Stockholm, Sweden.
Symbioses between diatoms and the N2-fixing, heterocyst-forming cyanobacterium Richelia spp. are widespread and contribute to primary production. Unique to these symbioses is a variation in the symbiont location: one lives in the host cytoplasm (endobiont) vs.
View Article and Find Full Text PDFACS Synth Biol
September 2025
Department of Medicinal Chemistry, Center for Natural Products, Drug Discovery and Development (CNPD3), University of Florida, Gainesville, Florida 32610, United States.
Heterologous expression of biosynthetic gene clusters (BGCs) is a powerful strategy for natural product (NP) discovery, yet achieving consistent expression across microbial hosts remains challenging. Here, we developed cross-phyla vector systems enabling the expression of BGCs from cyanobacteria and other bacterial origins in Gram-negative , Gram-positive , and two model cyanobacterial strains including unicellular PCC 6803 and filamentous sp. PCC 7120.
View Article and Find Full Text PDFMicrob Cell Fact
August 2025
Molecular Plant Biology Unit, Department of Life Technologies, University of Turku, Turku, Finland.
Cyanobacteria are emerging as a promising platform for whole-cell biotransformation, harnessing solar energy to drive biocatalytic reactions through recombinant enzymes. However, optimisation remains challenging due to the complexity of the cyanobacterial metabolism and the regulatory framework in which heterologous enzymes operate. While many enzymes have been deployed for light-driven whole-cell biotransformations, the different experimental conditions used between studies make direct comparison and systematic improvement difficult.
View Article and Find Full Text PDFBioresour Technol
August 2025
Helmholtz Center for Environmental Research (UFZ) Leipzig, Permoserstraße 15, D-04318, Germany.
Photosynthetic efficiency (PE) is key to evaluating phototrophic organisms in biotechnological applications. However, current methods offer limited, indirect insights with poor time resolution. To address this, photo-calorespirometry (Photo-CR) was developed, a novel, non-invasive technique for real-time, direct quantification of photosynthetic energy conversion.
View Article and Find Full Text PDFPlant Physiol Biochem
August 2025
Institute of Plant Biology, HUN-REN Biological Research Centre, Szeged, Temesvári krt. 62, H-6726, Szeged, Hungary. Electronic address:
Carotenoid biosynthesis in photosynthetic organisms involves converting cis-isomers to trans forms through enzymatic and light-induced reactions. While enzymatic pathways are well-documented, the role of light, particularly chlorophyll-mediated sensitization, remains unclear. This gap in understanding complicates efforts to optimize carotenoid production and fully grasp the evolutionary interplay between enzymatic and light-driven processes.
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