Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
| Autor: | Robert H. Wilson, Cai Zhen, Yin Li, Junli Zhang, Guoxia Liu, Alonso I. Carvajal |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
inorganic chemicals
Oxygenase Technology Rubisco Biomedical Engineering TP1-1185 Random hexamer Photosynthesis chemistry.chemical_compound Form II Hexamer Riftia pachyptila endosymbiont Ribulose 1 5-bisphosphate biology Renewable Energy Sustainability and the Environment Chemistry Chemical technology Carbon fixation RuBisCO fungi food and beverages Pyruvate carboxylase Biochemistry Carboxylation biology.protein CO2 capture in vivo TP248.13-248.65 Food Science Biotechnology |
| Zdroj: | Bioresources and Bioprocessing, Vol 8, Iss 1, Pp 1-16 (2021) |
| ISSN: | 2197-4365 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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