Enzyme Active Site Loop Revealed as a Gatekeeper for Cofactor Flip by Targeted Molecular Dynamics Simulations and FRET-Based Kinetics-Reference-Cited by-同舟云学术

Enzyme Active Site Loop Revealed as a Gatekeeper for Cofactor Flip by Targeted Molecular Dynamics Simulations and FRET-Based Kinetics

Published:2019-01-03 Issue:2 Volume:9 Page:1337-1346
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Rahuel-Clermont Sophie¹^ORCID,Bchini Raphaël¹,Barbe Sophie²,Boutserin Séverine¹,André Isabelle²^ORCID,Talfournier François¹

Affiliation:

1. Université de Lorraine, CNRS, IMoPA, Campus Biologie Santé, F-54000 Nancy, France

2. Laboratoire d’Ingénierie des Systèmes Biologiques et Procédés, LISBP, Université de Toulouse, CNRS, INRA, INSA, Toulouse, France, 135, Avenue de Rangueil, F-31077 Toulouse cedex 04, France

Funder

Universit? de Lorraine

Centre National de la Recherche Scientifique

R?gion Grand Est

Minist?re de l'Enseignement sup?rieur, de la Recherche et de l'Innovation

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.8b03951

Reference47 articles.

1. Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes

2. Role of Conformational Motions in Enzyme Function: Selected Methodologies and Case Studies

3. Coupled motions in enzyme catalysis

4. Enzyme Dynamics During Catalysis

5. Transient Catalytic Voltammetry of Sulfite Oxidase Reveals Rate Limiting Conformational Changes

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