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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 7, 2021
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.
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DOI of Published Version
https://doi.org/10.1186/s40643-021-00439-6
