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Microbiology
3 Results
- Research ArticleOpen Access
Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls d and f
Journal of Biological ChemistryVol. 298Issue 1101424Published online: November 18, 2021- Christopher J. Gisriel
- Gaozhong Shen
- Ming-Yang Ho
- Vasily Kurashov
- David A. Flesher
- Jimin Wang
- and others
Cited in Scopus: 16Far-red light (FRL) photoacclimation in cyanobacteria provides a selective growth advantage for some terrestrial cyanobacteria by expanding the range of photosynthetically active radiation to include far-red/near-infrared light (700–800 nm). During this photoacclimation process, photosystem II (PSII), the water:plastoquinone photooxidoreductase involved in oxygenic photosynthesis, is modified. The resulting FRL-PSII is comprised of FRL-specific core subunits and binds chlorophyll (Chl) d and Chl f molecules in place of several of the Chl a molecules found when cells are grown in visible light. - Research ArticleOpen Access
Structure of a photosystem I-ferredoxin complex from a marine cyanobacterium provides insights into far-red light photoacclimation
Journal of Biological ChemistryVol. 298Issue 1101408Published online: November 15, 2021- Christopher J. Gisriel
- David A. Flesher
- Gaozhong Shen
- Jimin Wang
- Ming-Yang Ho
- Gary W. Brudvig
- and others
Cited in Scopus: 7Far-red light photoacclimation exhibited by some cyanobacteria allows these organisms to use the far-red region of the solar spectrum (700–800 nm) for photosynthesis. Part of this process includes the replacement of six photosystem I (PSI) subunits with isoforms that confer the binding of chlorophyll (Chl) f molecules that absorb far-red light (FRL). However, the exact sites at which Chl f molecules are bound are still challenging to determine. To aid in the identification of Chl f-binding sites, we solved the cryo-EM structure of PSI from far-red light-acclimated cells of the cyanobacterium Synechococcus sp. - Microbiology MetabolismOpen Access
Biochemical Validation of the Glyoxylate Cycle in the Cyanobacterium Chlorogloeopsis fritschii Strain PCC 9212
Journal of Biological ChemistryVol. 290Issue 22p14019–14030Published online: April 13, 2015- Shuyi Zhang
- Donald A. Bryant
Cited in Scopus: 52Cyanobacteria are important photoautotrophic bacteria with extensive but variable metabolic capacities. The existence of the glyoxylate cycle, a variant of the TCA cycle, is still poorly documented in cyanobacteria. Previous studies reported the activities of isocitrate lyase and malate synthase, the key enzymes of the glyoxylate cycle in some cyanobacteria, but other studies concluded that these enzymes are missing. In this study the genes encoding isocitrate lyase and malate synthase from Chlorogloeopsis fritschii PCC 9212 were identified, and the recombinant enzymes were biochemically characterized.