ArticlePhotosynthesis research2008
Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic cyanobacterium Thermosynechococcus elongatus.
Article in Photosynthesis research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Chemoautotrophy in subzero environments and the potential for cold-adapted Rubisco.Applied and environmental microbiology · 2025Article
- Review
- Evolutionary Dynamics of RuBisCO: Emergence of the Small Subunit and its Impact Through Time.Molecular biology and evolution · 2025Article
- DnaK and DnaJ proteins from Hsp70/40 family are involved in Rubisco biosynthesis in Synechocystis sp. PCC6803 and sustain the enzyme assembly in a heterologous system.BMC plant biology · 2023Article
- Comparative Genomic Analysis Revealed Distinct Molecular Components and Organization of COFrontiers in microbiology · 2022Article
- Article
- Erythromycin Treatment ofLife (Basel, Switzerland) · 2020Article
- Revisiting Trade-offs between Rubisco Kinetic Parameters.Biochemistry · 2019Article
- Is RAF1 protein from Synechocystis sp. PCC 6803 really needed in the cyanobacterial Rubisco assembly process?Photosynthesis research · 2017Article
- A compendium of temperature responses of Rubisco kinetic traits: variability among and within photosynthetic groups and impacts on photosynthesis modeling.Journal of experimental botany · 2016Article
- Unlocking the Constraints of Cyanobacterial Productivity: Acclimations Enabling Ultrafast Growth.mBio · 2016Article
- Enhanced chloroplastic generation of H2O2 in stress-resistant Thellungiella salsuginea in comparison to Arabidopsis thaliana.Physiologia plantarum · 2015Article
- Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) can be divided into two branches: the "red-like type" of marine algae and the "green-like type" of cyanobacteria, green algae, and higher plants. We found that the "green-like type" rubisco from the thermophilic cyanobacterium Thermosynechococcus elongatus has an almost 2-fold higher specificity factor compared with rubiscos of mesophilic cyanobacteria, reaching the values of higher plants, and simultaneously revealing an improvement in enzyme thermostability. The difference in the activation energies at the transition stages between the oxygenase and carboxylase reactions for Thermosynechococcus elongatus rubisco is very close to that of Galdieria partita and significantly higher than that of spinach. This is the first characterization of a "green-like type" rubisco from thermophilic organism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.