Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture

Junli Zhang; Guoxia Liu; Alonso I Carvajal; Robert H Wilson; Zhen Cai; Yin Li

doi:10.1186/s40643-021-00439-6

Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO₂ capture

Bioresour Bioprocess. 2021 Sep 7;8(1):86. doi: 10.1186/s40643-021-00439-6.

Authors

Junli Zhang^#^{1

2}, Guoxia Liu^#¹, Alonso I Carvajal³, Robert H Wilson^{4

5}, Zhen Cai⁶, Yin Li⁷

Affiliations

¹ CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
² University of the Chinese Academy of Sciences, Beijing, China.
³ Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.
⁴ Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany. rhwilson@mit.edu.
⁵ Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA. rhwilson@mit.edu.
⁶ CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. caiz@im.ac.cn.
⁷ CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. yli@im.ac.cn.

^# Contributed equally.

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.

Keywords: Riftia pachyptila endosymbiont; CO2 capture in vivo; Form II; Hexamer; Rubisco.

Grants and funding

2150060111/the National Natural Science Foundation of China