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Ribulose 1,5- bisphosphate carboxylase/oxygenase (RuBisCo) is a critical enzyme that catalyzes carbon dioxide assimilation during photosynthesis. However, it is an inefficient enzyme, having an extremely slow catalytic rate. A typical enzyme can process about a thousand molecules per second; however, RuBisCo fixes only around three-carbon dioxides per second. Photosynthetic cells compensate for this slow rate by synthesizing very high amounts of RuBisCo, making it the most abundant single...
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Engineering Rubisco to enhance CO2 utilization.

Lei Zhao1,2, Zhen Cai1, Yin Li1

  • 1CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.

Synthetic and Systems Biotechnology
|January 26, 2024
PubMed
Summary
This summary is machine-generated.

Improving carbon fixation involves modifying Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the most abundant enzyme. Heterologous expression in microorganisms enables evaluation and directed evolution of high-performance Rubisco mutants for enhanced carbon capture.

Keywords:
Carbon fixation pathwayEnzyme engineeringMicrobialPlant CO2 fixationRubiscoSynthetic biology

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is crucial for CO2 fixation and global biogeochemical cycles.
  • Low carboxylation and high oxygenase activity limit Rubisco's efficiency in carbon fixation.
  • Direct modification of plant Rubisco is hindered by conservation and chloroplast transformation challenges.

Purpose of the Study:

  • To review current strategies for modifying plant Rubisco.
  • To highlight advancements in Rubisco biogenesis and heterologous expression.
  • To explore the potential of engineered Rubisco in microorganisms for carbon fixation and biotransformation.

Main Methods:

  • Review of existing literature on Rubisco modification and engineering.
  • Discussion of chaperone-assisted Rubisco biogenesis.
  • Overview of heterologous expression systems, including E. coli screening.

Main Results:

  • Successful heterologous expression of diverse Rubisco forms in microorganisms is now feasible.
  • Chaperone-assisted biogenesis aids in understanding and producing functional Rubisco.
  • Directed evolution in E. coli offers a pathway to high-performance Rubisco mutants.

Conclusions:

  • Heterologous expression and directed evolution in microorganisms overcome previous limitations in Rubisco modification.
  • Engineered Rubisco in microbes can enhance carbon fixation capabilities.
  • This approach holds significant potential for improving biotransformation processes and carbon capture technologies.