Photosystem II (PSII) is a large membrane protein complex that uses light to split water into molecular oxygen, protons, and electrons. Here we report the (1)H, (15)N and (13)C backbone chemical shift assignments for the Psb27 protein of Photosystem II from Synechocystis PCC 6803. These assignments will now provide the basis for the structural analysis of the Psb27 protein.
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http://dx.doi.org/10.1007/s12104-009-9186-0 | DOI Listing |
Appl Biochem Biotechnol
January 2025
Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Cyanobacteria are advantageous hosts for industrial applications toward achieving sustainable society due to their unique and superior properties such as atmospheric CO fixation via photosynthesis. However, cyanobacterial productivities tend to be weak compared to heterotrophic microbes. To enhance them, it is necessary to understand the fundamental metabolic mechanisms unique to cyanobacteria.
View Article and Find Full Text PDFEnviron Sci Ecotechnol
January 2025
Systems Biotechnology Group, Department of Microbial Biotechnology, Helmholtz Centre for Environmental Research - UFZ, 04318, Leipzig, Germany.
Biophotovoltaics (BPV) represents an innovative biohybrid technology that couples electrochemistry with oxygenic photosynthetic microbes to harness solar energy and convert it into electricity. Central to BPV systems is the ability of microbes to perform extracellular electron transfer (EET), utilizing an anode as an external electron sink. This process simultaneously serves as an electron sink and enhances the efficiency of water photolysis compared to conventional electrochemical water splitting.
View Article and Find Full Text PDFFEBS J
January 2025
Department of Biological Sciences, Chungnam National University, Daejeon, Korea.
Previous studies have identified three families of knotted phytochrome photoreceptors in cyanobacteria. We describe a fourth type: 'hybrid' phytochromes with putative bilin-binding cysteine residues in both their N-terminal 'knot' extensions and cGMP-phosphodiesterase/adenylate cyclase/FhlA (GAF) domains, which we designate as dual-cysteine bacteriophytochromes (DCBs). Recombinant expression of DCBs in Escherichia coli yields photoactive phycocyanobilin (PCB) adducts with red/far-red photocycles similar to those of the GAF-Cys-containing cyanobacterial phytochromes (Cph1s).
View Article and Find Full Text PDFMicrobiol Res
January 2025
National Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China. Electronic address:
RNase III, a ubiquitously distributed endonuclease, plays an important role in RNA processing and functions as a global regulator of gene expression. In this study, we explored the role of RNase III in mediating the oxidative stress response in Synechocystis sp. PCC 6803.
View Article and Find Full Text PDFAntioxidants (Basel)
December 2024
Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.
Glutathione S-transferases (GSTs) are evolutionarily conserved enzymes crucial for cell detoxication. They are viewed as having evolved in cyanobacteria, the ancient photosynthetic prokaryotes that colonize our planet and play a crucial role for its biosphere. Xi-class GSTs, characterized by their specific glutathionyl-hydroquinone reductase activity, have been observed in prokaryotes, fungi and plants, but have not yet been studied in cyanobacteria.
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