Covalent Adduct Formation as a Strategy for Efficient CO<sub>2</sub> Fixation in Crotonyl-CoA Carboxylases/Reductases-Reference-Cited by-同舟云学术

Covalent Adduct Formation as a Strategy for Efficient CO₂ Fixation in Crotonyl-CoA Carboxylases/Reductases

Published:2023-04-21 Issue:9 Volume:13 Page:6230-6241
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Recabarren Rodrigo¹,Tinzl Matthias²,Saez David Adrian³^ORCID,Gomez Aharon¹^ORCID,Erb Tobias J.²⁴^ORCID,Vöhringer-Martinez Esteban¹^ORCID

Affiliation:

1. Departamento de Físico-Química, Facultad de Ciencias Químicas, Universidad de Concepción, 4030000 Concepción, Chile

2. Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Straße 10, D-35043 Marburg, Germany

3. Departamento de Farmacia, Facultad de Farmacia, Universidad de Concepción, 4030000 Concepción, Chile

4. LOEWE Center for Synthetic Microbiology (SYNMIKRO), 35032 Marburg, Germany

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Comisión Nacional de Investigación Científica y Tecnológica

Max-Planck-Gesellschaft

H2020 European Research Council

Fondo Nacional de Desarrollo Científico y Tecnológico

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.2c05250

Reference71 articles.

1. Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO2 Fixation

2. Catalysis and regulation in Rubisco

3. Mechanism of Rubisco: The Carbamate as General Base

4. The most abundant protein in the world

5. Four amino acids define the CO2binding pocket of enoyl-CoA carboxylases/reductases

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