Conformational Dynamics of the Most Efficient Carboxylase Contributes to Efficient CO<sub>2</sub> Fixation-Reference-Cited by-同舟云学术

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Conformational Dynamics of the Most Efficient Carboxylase Contributes to Efficient CO₂ Fixation

Published:2023-12-04 Issue:24 Volume:63 Page:7807-7815
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Gomez Aharon¹^ORCID,Erb Tobias J.²³^ORCID,Grubmüller Helmut⁴^ORCID,Vöhringer-Martinez Esteban¹^ORCID

Affiliation:

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

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

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

4. Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen D-37073, Germany

Funder

European Research Council

Consejo Nacional de Innovaci?n, Ciencia y Tecnolog?a

Max-Planck-Gesellschaft

Agencia Nacional de Investigaci?n y Desarrollo

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.3c01447

Reference33 articles.

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

2. Enzymatic Conversion of CO₂: From Natural to Artificial Utilization

3. Catalysis and regulation in Rubisco

4. Mechanism of Rubisco: The Carbamate as General Base

5. The most abundant protein in the world

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