scholarly journals Hydrogen production through oxygenic photosynthesis using the cyanobacterium Synechocystis sp. PCC 6803 in a bio-photoelectrolysis cell (BPE) system

2013 ◽  
Vol 6 (9) ◽  
pp. 2682 ◽  
Author(s):  
Alistair J. McCormick ◽  
Paolo Bombelli ◽  
David J. Lea-Smith ◽  
Robert W. Bradley ◽  
Amanda M. Scott ◽  
...  
2016 ◽  
Vol 41 (34) ◽  
pp. 15181-15186 ◽  
Author(s):  
Eleftherios Touloupakis ◽  
George Rontogiannis ◽  
Ana Margarita Silva Benavides ◽  
Bernardo Cicchi ◽  
Demetrios F. Ghanotakis ◽  
...  

2020 ◽  
Vol 40 (4) ◽  
Author(s):  
Lauren A. Mills ◽  
Alistair J. McCormick ◽  
David J. Lea-Smith

Abstract Cyanobacteria are key organisms in the global ecosystem, useful models for studying metabolic and physiological processes conserved in photosynthetic organisms, and potential renewable platforms for production of chemicals. Characterizing cyanobacterial metabolism and physiology is key to understanding their role in the environment and unlocking their potential for biotechnology applications. Many aspects of cyanobacterial biology differ from heterotrophic bacteria. For example, most cyanobacteria incorporate a series of internal thylakoid membranes where both oxygenic photosynthesis and respiration occur, while CO2 fixation takes place in specialized compartments termed carboxysomes. In this review, we provide a comprehensive summary of our knowledge on cyanobacterial physiology and the pathways in Synechocystis sp. PCC 6803 (Synechocystis) involved in biosynthesis of sugar-based metabolites, amino acids, nucleotides, lipids, cofactors, vitamins, isoprenoids, pigments and cell wall components, in addition to the proteins involved in metabolite transport. While some pathways are conserved between model cyanobacteria, such as Synechocystis, and model heterotrophic bacteria like Escherichia coli, many enzymes and/or pathways involved in the biosynthesis of key metabolites in cyanobacteria have not been completely characterized. These include pathways required for biosynthesis of chorismate and membrane lipids, nucleotides, several amino acids, vitamins and cofactors, and isoprenoids such as plastoquinone, carotenoids, and tocopherols. Moreover, our understanding of photorespiration, lipopolysaccharide assembly and transport, and degradation of lipids, sucrose, most vitamins and amino acids, and haem, is incomplete. We discuss tools that may aid our understanding of cyanobacterial metabolism, notably CyanoSource, a barcoded library of targeted Synechocystis mutants, which will significantly accelerate characterization of individual proteins.


2020 ◽  
Vol 1861 (8) ◽  
pp. 148208
Author(s):  
Daniela Kannchen ◽  
Jure Zabret ◽  
Regina Oworah-Nkruma ◽  
Nina Dyczmons-Nowaczyk ◽  
Katrin Wiegand ◽  
...  

2021 ◽  
Vol 22 (7) ◽  
pp. 3733
Author(s):  
Jana Knoppová ◽  
Jianfeng Yu ◽  
Jan Janouškovec ◽  
Petr Halada ◽  
Peter J. Nixon ◽  
...  

Photochemical energy conversion during oxygenic photosynthesis is performed by membrane-embedded chlorophyll-binding protein complexes. The biogenesis and maintenance of these complexes requires auxiliary protein factors that optimize the assembly process and protect nascent complexes from photodamage. In cyanobacteria, several lipoproteins contribute to the biogenesis and function of the photosystem II (PSII) complex. They include CyanoP, CyanoQ, and Psb27, which are all attached to the lumenal side of PSII complexes. Here, we show that the lumenal Ycf48 assembly factor found in the cyanobacterium Synechocystis sp. PCC 6803 is also a lipoprotein. Detailed mass spectrometric analysis of the isolated protein supported by site-directed mutagenesis experiments indicates lipidation of the N-terminal C29 residue of Ycf48 and removal of three amino acids from the C-terminus. The lipobox sequence in Ycf48 contains a cysteine residue at the −3 position compared to Leu/Val/Ile residues found in the canonical lipobox sequence. The atypical Ycf48 lipobox sequence is present in most cyanobacteria but is absent in eukaryotes. A possible role for lipoproteins in the coordinated assembly of cyanobacterial PSII is discussed.


2021 ◽  
Vol 12 ◽  
Author(s):  
Stefan Lucius ◽  
Alexander Makowka ◽  
Klaudia Michl ◽  
Kirstin Gutekunst ◽  
Martin Hagemann

Cyanobacteria perform plant-like oxygenic photosynthesis to convert inorganic carbon into organic compounds and can also use internal carbohydrate reserves under specific conditions. A mutant collection with defects in different routes for sugar catabolism was studied to analyze which of them is preferentially used to degrade glycogen reserves in light-exposed cells of Synechocystis sp. PCC 6803 shifted from high to low CO2 conditions. Mutants defective in the glycolytic Embden–Meyerhof–Parnas pathway or in the oxidative pentose-phosphate (OPP) pathway showed glycogen levels similar to wild type under high CO2 (HC) conditions and were able to degrade it similarly after shifts to low CO2 (LC) conditions. In contrast, the mutant Δeda, which is defective in the glycolytic Entner-Doudoroff (ED) pathway, accumulated elevated glycogen levels under HC that were more slowly consumed during the LC shift. In consequence, the mutant Δeda showed a lowered ability to respond to the inorganic carbon shifts, displayed a pronounced lack in the reactivation of growth when brought back to HC, and differed significantly in its metabolite composition. Particularly, Δeda accumulated enhanced levels of proline, which is a well-known metabolite to maintain redox balances via NADPH levels in many organisms under stress conditions. We suggest that deletion of eda might promote the utilization of the OPP shunt that dramatically enhance NADPH levels. Collectively, the results point at a major regulatory contribution of the ED pathway for the mobilization of glycogen reserves during rapid acclimation to fluctuating CO2 conditions.


Microbiology ◽  
2012 ◽  
Vol 158 (2) ◽  
pp. 448-464 ◽  
Author(s):  
Filipe Pinto ◽  
Karin A. van Elburg ◽  
Catarina C. Pacheco ◽  
Miguel Lopo ◽  
Josselin Noirel ◽  
...  

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