ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2008
Phylogenetic and evolutionary relationships of RubisCO and the RubisCO-like proteins and the functional lessons provided by diverse molecular forms.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 159 citations in OpenAlex.
- Rubisco is slow across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- A systematic exploration of bacterial form I rubisco maximal carboxylation rates.The EMBO journal · 2024Article
- Rubisco is evolving for improved catalytic efficiency and COProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Microbial metabolic potential of hydrothermal vent chimneys along the submarine ring of fire.Frontiers in microbiology · 2024Article
- Multi-environment ecogenomics analysis of the cosmopolitan phylum Gemmatimonadota.Microbiology spectrum · 2023Article
- Red Rubiscos and opportunities for engineering green plants.Journal of experimental botany · 2023Review
- A robust approach to estimate relative phytoplankton cell abundances from metagenomes.Molecular ecology resources · 2023Article
- Article
- Atypical Carboxysome Loci: JEEPs or Junk?Frontiers in microbiology · 2022Review
- An Insight of RuBisCO Evolution through a Multilevel Approach.Biomolecules · 2021Article
- Transcriptome-Wide Gene Expression Plasticity inInternational journal of molecular sciences · 2021Article
- The MpsAB Bicarbonate Transporter Is Superior to Carbonic Anhydrase in Biofilm-Forming Bacteria with Limited COMicrobiology spectrum · 2021Article
- Candidatus Eremiobacterota, a metabolically and phylogenetically diverse terrestrial phylum with acid-tolerant adaptations.The ISME journal · 2021Article
- Article
- The curious consistency of carbon biosignatures over billions of years of Earth-life coevolution.The ISME journal · 2021Review
- Photorespiration: The Futile Cycle?Plants (Basel, Switzerland) · 2021Review
- Common Presence of PhototrophicmSystems · 2021Article
- Wide range of metabolic adaptations to the acquisition of the Calvin cycle revealed by comparison of microbial genomes.PLoS computational biology · 2021Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RubisCO) catalyses the key reaction by which inorganic carbon may be assimilated into organic carbon. Phylogenetic analyses indicate that there are three classes of bona fide RubisCO proteins, forms I, II and III, which all catalyse the same reactions. In addition, there exists another form of RubisCO, form IV, which does not catalyse RuBP carboxylation or oxygenation. Form IV is actually a homologue of RubisCO and is called the RubisCO-like protein (RLP). Both RubisCO and RLP appear to have evolved from an ancestor protein in a methanogenic archaeon, and comprehensive analyses indicate that the different forms (I, II, III and IV) contain various subgroups, with individual sequences derived from representatives of all three kingdoms of life. The diversity of RubisCO molecules, many of which function in distinct milieus, has provided convenient model systems to study the ways in which the active site of this protein has evolved to accommodate necessary molecular adaptations. Such studies have proven useful to help provide a framework for understanding the molecular basis for many important aspects of RubisCO catalysis, including the elucidation of factors or functional groups that impinge on RubisCO carbon dioxide/oxygen substrate discrimination.
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