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

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

SUBMITTER: Zhang J 

PROVIDER: S-EPMC10992382 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature