Infrared spectroscopy reveals metal-independent carbonic anhydrase activity in crotonyl-CoA carboxylase/reductase-Reference-Cited by-同舟云学术

Infrared spectroscopy reveals metal-independent carbonic anhydrase activity in crotonyl-CoA carboxylase/reductase

Published:2024 Issue:13 Volume:15 Page:4960-4968
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Gomez Aharon¹^ORCID,Tinzl Matthias²,Stoffel Gabriele²,Westedt Hendrik²,Grubmüller Helmut³,Erb Tobias J.²⁴,Vöhringer-Martinez Esteban¹^ORCID,Stripp Sven T.⁵⁶^ORCID

Affiliation:

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

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

3. Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Multidisciplinary Sciences, Am Fassberg 11, 37077 Göttingen, Germany

4. Center for Synthetic Microbiology (SYNMIKRO), Germany

5. Freie Universität Berlin, Experimental Molecular Biophysics, Arnimallee 14, 14195 Berlin, Germany

6. Technische Universität Berlin, Division of Physical Chemistry, Strasse des 17. Juni 124, 10623 Berlin, Germany

Abstract

Using infrared spectroscopy and molecular simulations we show that the fastest CO2-fixing enzyme found in nature has an unknown anhydrase activity in absence of substrate.

Funder

Max-Planck-Gesellschaft

Agencia Nacional de Investigación y Desarrollo

Max-Planck-Institut für Terrestrische Mikrobiologie

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

European Research Council

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D3SC04208A

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