ArticlePloS one2015
Serine 363 of a Hydrophobic Region of Archaeal Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from Archaeoglobus fulgidus and Thermococcus kodakaraensis Affects CO2/O2 Substrate Specificity and Oxygen Sensitivity.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 23 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
- Highly active rubiscos discovered by systematic interrogation of natural sequence diversity.The EMBO journal · 2020Article
- Selection of Cyanobacterial (mBio · 2019Article
- Photoreduction of COJournal of the American Chemical Society · 2018Article
- Synthetic COBiotechnology for biofuels · 2017Article
- A synthetic pathway for the fixation of carbon dioxide in vitro.Science (New York, N.Y.) · 2016Article
- Biochemical and synthetic biology approaches to improve photosynthetic COCurrent opinion in chemical biology · 2016Review
- RubisCO selection using the vigorously aerobic and metabolically versatile bacterium Ralstonia eutropha.The FEBS journal · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Archaeal ribulose 1, 5-bisphospate carboxylase/oxygenase (RubisCO) is differentiated from other RubisCO enzymes and is classified as a form III enzyme, as opposed to the form I and form II RubisCOs typical of chemoautotrophic bacteria and prokaryotic and eukaryotic phototrophs. The form III enzyme from archaea is particularly interesting as several of these proteins exhibit unusual and reversible sensitivity to molecular oxygen, including the enzyme from Archaeoglobus fulgidus. Previous studies with A. fulgidus RbcL2 had shown the importance of Met-295 in oxygen sensitivity and pointed towards the potential significance of another residue (Ser-363) found in a hydrophobic pocket that is conserved in all RubisCO proteins. In the current study, further structure/function studies have been performed focusing on Ser-363 of A. fulgidus RbcL2; various changes in this and other residues of the hydrophobic pocket point to and definitively establish the importance of Ser-363 with respect to interactions with oxygen. In addition, previous findings had indicated discrepant CO2/O2 specificity determinations of the Thermococcus kodakaraensis RubisCO, a close homolog of A. fulgidus RbcL2. It is shown here that the T. kodakaraensis enzyme exhibits a similar substrate specificity as the A. fulgidus enzyme and is also oxygen sensitive, with equivalent residues involved in oxygen interactions.
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