ArticleJournal of bacteriology2003
Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 75 citations in OpenAlex.
- Not just Rubisco: integrated strategies to overcome the biochemical limitations of CFrontiers in plant science · 2026Review
- Form III RubisCO-mediated transaldolase variant of the Calvin cycle in a chemolithoautotrophic bacterium.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Prodigal Compound: Return of Ribosyl 1,5-Bisphosphate as an Important Player in Metabolism.Microbiology and molecular biology reviews : MMBR · 2019Review
- The Arnon-Buchanan cycle: a retrospective, 1966-2016.Photosynthesis research · 2017Article
- A unique structural domain inThe Journal of biological chemistry · 2017Article
- A peptide adhesive molded by magnesium glues Rubisco's subunits together.The Journal of biological chemistry · 2017Article
- RubisCO of a nucleoside pathway known from Archaea is found in diverse uncultivated phyla in bacteria.The ISME journal · 2016Article
- Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.Environmental microbiology · 2016Article
- A pentose bisphosphate pathway for nucleoside degradation in Archaea.Nature chemical biology · 2015Article
- Article
- Tandem repeats, high copy number and remarkable diel expression rhythm of form II RuBisCO in Prorocentrum donghaiense (Dinophyceae).PloS one · 2013Article
- Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway.Journal of bacteriology · 2012Article
- Proteome analyses of hydrogen-producing hyperthermophilic archaeon Thermococcus onnurineus NA1 in different one-carbon substrate culture conditions.Molecular & cellular proteomics : MCP · 2012Article
- The biological deep sea hydrothermal vent as a model to study carbon dioxide capturing enzymes.Marine drugs · 2011Review
- Structure-based catalytic optimization of a type III Rubisco from a hyperthermophile.The Journal of biological chemistry · 2010Article
- Autotrophic carbon fixation in archaea.Nature reviews. Microbiology · 2010Review
- Substrate-induced assembly of Methanococcoides burtonii D-ribulose-1,5-bisphosphate carboxylase/oxygenase dimers into decamers.The Journal of biological chemistry · 2009Article
- A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.Biochemistry · 2009Article
- Expression and regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase genes in Mycobacterium sp. strain JC1 DSM 3803.Journal of microbiology (Seoul, Korea) · 2009Article
- Structural and functional similarities between a ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)-like protein from Bacillus subtilis and photosynthetic RuBisCO.The Journal of biological chemistry · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ribulose 1,5 bisphosphate carboxylase/oxygenase (RubisCO) catalyzes the biological reduction and assimilation of carbon dioxide gas to organic carbon; it is the key enzyme responsible for the bulk of organic matter found on earth. Until recently it was believed that there are only two forms of RubisCO, form I and form II. However, the recent completion of several genome-sequencing projects uncovered open reading frames resembling RubisCO in the third domain of life, the archaea. Previous work and homology comparisons suggest that these enzymes represent a third form of RubisCO, form III. While earlier work indicated that two structurally distinct recombinant archaeal RubisCO proteins catalyzed bona fide RubisCO reactions, it was not established that the rbcL genes of anaerobic archaea can be transcribed and translated to an active enzyme in the native organisms. In this report, it is shown not only that Methanococcus jannaschii, Archaeoglobus fulgidus, Methanosarcina acetivorans, and Methanosarcina barkeri possess open reading frames with the residues required for catalysis but also that the RubisCO protein from these archaea accumulates in an active form under normal growth conditions. In addition, the form III RubisCO gene (rbcL) from M. acetivorans was shown to complement RubisCO deletion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under both photoheterotrophic and photoautotrophic growth conditions. These studies thus indicate for the first time that archaeal form III RubisCO functions in a physiologically significant fashion to fix CO(2). Furthermore, recombinant M. jannaschii, M. acetivorans, and A. fulgidus RubisCO possess unique properties with respect to quaternary structure, temperature optima, and activity in the presence of molecular oxygen compared to the previously described Thermococcus kodakaraensis and halophile proteins.
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