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), whic...

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Main Authors:	Junli Zhang, Guoxia Liu, Alonso I. Carvajal, Robert H. Wilson, Zhen Cai, Yin Li
Format:	Article
Language:	English
Published:	SpringerOpen 2021-09-01
Series:	Bioresources and Bioprocessing
Subjects:	Rubisco Riftia pachyptila endosymbiont Form II Hexamer CO2 capture in vivo
Online Access:	https://doi.org/10.1186/s40643-021-00439-6

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record_format	Article
spelling	doaj-40c4ff0bede541a2b7a41c7e7eb396162021-09-12T11:04:00ZengSpringerOpenBioresources and Bioprocessing2197-43652021-09-018111610.1186/s40643-021-00439-6Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 captureJunli Zhang0Guoxia Liu1Alonso I. Carvajal2Robert H. Wilson3Zhen Cai4Yin Li5CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of SciencesDepartment of Cellular Biochemistry, Max Planck Institute of BiochemistryDepartment of Cellular Biochemistry, Max Planck Institute of BiochemistryCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of SciencesCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of SciencesAbstract 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.https://doi.org/10.1186/s40643-021-00439-6RubiscoRiftia pachyptila endosymbiontForm IIHexamerCO2 capture in vivo
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Junli Zhang Guoxia Liu Alonso I. Carvajal Robert H. Wilson Zhen Cai Yin Li
spellingShingle	Junli Zhang Guoxia Liu Alonso I. Carvajal Robert H. Wilson Zhen Cai Yin Li Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture Bioresources and Bioprocessing Rubisco Riftia pachyptila endosymbiont Form II Hexamer CO2 capture in vivo
author_facet	Junli Zhang Guoxia Liu Alonso I. Carvajal Robert H. Wilson Zhen Cai Yin Li
author_sort	Junli Zhang
title	Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
title_short	Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
title_full	Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
title_fullStr	Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
title_full_unstemmed	Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture
title_sort	discovery of a readily heterologously expressed rubisco from the deep sea with potential for co2 capture
publisher	SpringerOpen
series	Bioresources and Bioprocessing
issn	2197-4365
publishDate	2021-09-01
description	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.
topic	Rubisco Riftia pachyptila endosymbiont Form II Hexamer CO2 capture in vivo
url	https://doi.org/10.1186/s40643-021-00439-6
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Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture

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