Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
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40643_2021_Article_439.pdf
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Author(s)
Zhang, Junli
Liu, Guoxia
Carvajal, Alonso I.
Wilson, Robert H.
Cai, Zhen
Li, Yin
Date Issued
September 2021
Journal
Bioresources and Bioprocessing
Publisher
Springer Singapore
Citation
Bioresources and Bioprocessing. 2021 Sep 07;8(1):86
Version
Final published version
Abstract
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the key CO2-fixing enzyme in photosynthesis, is notorious for its low carboxylation. We report a highly active and assembly-competent Form II Rubisco from the endosymbiont of a deep-sea tubeworm Riftia pachyptila (RPE Rubisco), which shows a 50.5% higher carboxylation efficiency than that of a high functioning Rubisco from Synechococcus sp. PCC7002 (7002 Rubisco). It is a simpler hexamer with three pairs of large subunit homodimers around a central threefold symmetry axis. Compared with 7002 Rubisco, it showed a 3.6-fold higher carbon capture efficiency in vivo using a designed CO2 capture model. The simple structure, high carboxylation efficiency, easy heterologous soluble expression/assembly make RPE Rubisco a ready-to-deploy enzyme for CO2 capture that does not require complex co-expression of chaperones. The chemosynthetic CO2 fixation machinery of chemolithoautotrophs, CO2-fixing endosymbionts, may be more efficient than previously realized with great potential for next-generation microbial CO2 sequestration platforms.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.1186/s40643-021-00439-6
