ArticleBiochemistry2009
A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- The fitness landscape of a form II rubisco in a photosynthetic bacterium guides engineering of oxygen tolerance.Science advances · 2026Article
- High-Throughput Detection of Cyanobacterial Form I Rubisco Assembly.ACS synthetic biology · 2026Article
- Strategies to improve photosynthesis by modifying the RuBisCO system and its limitations.Molecular biology reports · 2025Review
- A Cyanobacterial Screening Platform for Rubisco Mutant Variants.ACS synthetic biology · 2025Article
- In vivo directed evolution of an ultrafast Rubisco from a semianaerobic environment imparts oxygen resistance.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024Review
- Directed Evolution of an Improved Rubisco; In Vitro Analyses to Decipher Fact from Fiction.International journal of molecular sciences · 2019Article
- Selection of Cyanobacterial (mBio · 2019Article
- Directed -in vitro- evolution of Precambrian and extant Rubiscos.Scientific reports · 2018Article
- Global metabolic rewiring for improved CONature communications · 2017Article
- RubisCO of a nucleoside pathway known from Archaea is found in diverse uncultivated phyla in bacteria.The ISME journal · 2016Article
- RubisCO selection using the vigorously aerobic and metabolically versatile bacterium Ralstonia eutropha.The FEBS journal · 2016Article
- Article
- Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria.Environmental microbiology · 2016Article
- In Vivo Studies in Rhodospirillum rubrum Indicate That Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Catalyzes Two Obligatorily Required and Physiologically Significant Reactions for Distinct Carbon and Sulfur Metabolic Pathways.The Journal of biological chemistry · 2015Article
- Article
- Structure-function studies with the unique hexameric form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Rhodopseudomonas palustris.The Journal of biological chemistry · 2014Article
- Development of an activity-directed selection system enabled significant improvement of the carboxylation efficiency of Rubisco.Protein & cell · 2014Article
- Structure and identification of a pterin dehydratase-like protein as a ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) assembly factor in the α-carboxysome.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) is a globally significant biocatalyst that facilitates the removal and sequestration of CO2 from the biosphere. Rubisco-catalyzed CO2 reduction thus provides virtually all of the organic carbon utilized by living organisms. Despite catalyzing the rate-limiting step of photosynthetic and chemoautotrophic CO2 assimilation, Rubisco is markedly inefficient as the competition between O2 and CO2 for the same substrate limits the ability of aerobic organisms to obtain maximum amounts of organic carbon for CO2-dependent growth. Random and site-directed mutagenesis procedures were coupled with genetic selection to identify an "oxygen-insensitive" mutant cyanobacterial (Synechococcus sp. strain PCC 6301) Rubisco that allowed for CO2-dependent growth of a host bacterium at an oxygen concentration that inhibited growth of the host containing wild-type Synechococcus Rubisco. The mutant substitution, A375V, was identified as an intragenic suppressor of D103V, a negative mutant enzyme incapable of supporting autotrophic growth. Ala-375 (Ala-378 of spinach Rubisco) is a conserved residue in all form I (plant-like) Rubiscos. Structure-function analyses indicate that the A375V substitution decreased the enzyme's oxygen sensitivity (and not CO2/O2 specificity), possibly by rearranging a network of interactions in a fairly conserved hydrophobic pocket near the active site. These studies point to the potential of engineering plants and other significant aerobic organisms to fix CO2 unfettered by the presence of O2.
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Registered trials
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.