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Intersubunit Coupling Enables Fast CO2-Fixation by Reductive Carboxylases.

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Enoyl-CoA carboxylases/reductases (ECRs) are efficient CO2-fixing enzymes. This study reveals how synchronized protein dynamics in Kitasatospora setae ECRs enable rapid carbon fixation through coupled catalytic domains.

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Area of Science:

  • Biochemistry and structural biology
  • Enzyme kinetics and mechanisms
  • Molecular enzymology

Background:

  • Enoyl-CoA carboxylases/reductases (ECRs) are highly efficient carbon dioxide (CO2)-fixing enzymes.
  • The precise molecular mechanisms governing ECRs' catalytic prowess at the protein assembly level are not fully understood.

Purpose of the Study:

  • To elucidate the structural organization and dynamic mechanisms of the ECR from Kitasatospora setae.
  • To understand how protein assembly and subunit communication contribute to high CO2-fixation rates.

Main Methods:

  • Ambient-temperature X-ray free electron laser (XFEL) and cryogenic synchrotron experiments.
  • Molecular dynamics simulations.
  • Structure-based mutagenesis.

Main Results:

  • Kitasatospora setae ECR functions as a homotetramer, existing as open- and closed-form dimers in the active state.
  • Catalysis is synchronized across the dimer pairs, driven by conformational coupling of catalytic domains.
  • Specific amino acids are crucial for conferring this conformational coupling and high CO2 fixation.

Conclusions:

  • The study provides unprecedented insights into the dynamic organization of ECRs.
  • Synchronized inter- and intra-subunit communication is key to the enzyme's remarkable efficiency.
  • Understanding these mechanisms can inform the design of novel carbon-fixing technologies.