Ternary Complex Formation and Photoactivation of a Photoenzyme Results in Altered Protein Dynamics-Reference-Cited by-同舟云学术

Ternary Complex Formation and Photoactivation of a Photoenzyme Results in Altered Protein Dynamics

Published:2019-08-05 Issue:34 Volume:123 Page:7372-7384
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Stadler Andreas Maximilian^ORCID,Schneidewind Judith,Zamponi Michaela¹,Knieps-Grünhagen Esther,Gholami Samira²^ORCID,Schwaneberg Ulrich³⁴^ORCID,Rivalta Ivan⁵^ORCID,Garavelli Marco²⁶^ORCID,Davari Mehdi D.³^ORCID,Jaeger Karl-Erich⁷^ORCID,Krauss Ulrich^ORCID

Affiliation:

1. Jülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH, Lichtenbergstr. 1, 85748 Garching, Germany

2. Dipartimento di Chimica Industriale, Università degli Studi di Bologna, Viale del Risorgimento 4, I-40136 Bologna, Italy

3. Institute of Biotechnology, RWTH Aachen University, Worringer Weg 3, D-52074 Aachen, Germany

4. DWI-Leibniz Institute for Interactive Materials, Forckenbeckstraße 50, 52056 Aachen, Germany

5. Université de Lyon, École Normale Supérieure de Lyon, CNRS, Université Claude Bernard Lyon 1, Laboratoire de Chimie UMR 5182, F-69342 Lyon, France

6. École Normale Supérieure de Lyon, CNRS, Laboratoire de Chimie UMR 5182, Université de Lyon, 46 Allée d’Italie, F-69364 Lyon Cedex 07, France

7. IBG-1: Biotechnologie, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany

Funder

RWTH Aachen University

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.9b06608

Reference70 articles.

1. Effect of Conformational Dynamics on Substrate Recognition and Specificity as Probed by the Introduction of a de Novo Disulfide Bond into Cytochrome P450 2B1

2. Dynamics of the Dihydrofolate Reductase-Folate Complex: Catalytic Sites and Regions Known To Undergo Conformational Change Exhibit Diverse Dynamical Features

4. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase

5. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

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