QM/MM study of l-lactate oxidation by flavocytochrome b2-Reference-Cited by-同舟云学术

QM/MM study of l-lactate oxidation by flavocytochrome b2

Published:2016 Issue:23 Volume:18 Page:15609-15618
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Gillet N.¹²³⁴⁵,Ruiz-Pernía J. J.⁶⁷⁸⁹,de la Lande A.¹²³⁴⁵,Lévy B.¹²³⁴⁵,Lederer F.¹²³⁴⁵,Demachy I.¹²³⁴⁵,Moliner V.⁶⁷⁸⁹

Affiliation:

1. Laboratoire de Chimie-Physique

2. CNRS UMR 8000

3. Université Paris Sud

4. 91405 Cedex Orsay

5. France

6. Departament de Química Física i Analítica

7. Universitat Jaume I

8. 12071 Castellón

9. Spain

Abstract

Free energy surfaces calculated from a state-of-the-art computational methodology highlight the role of active site residues in l-lactate oxidation by flavocytochrome b₂.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CP/C6CP00395H

Reference58 articles.

1. F. Lederer , in Chemistry and biochemistry of flavoenzymes, ed. F. Müller, Boca Raton, CRC Press, 1991, vol. 2, pp. 153–242

2. Mechanisms of flavoprotein-catalyzed reactions

3. Crystallographic Study of the Recombinant Flavin-Binding Domain of Baker's Yeast Flavocytochrome b2: Comparison with the Intact Wild-Type Enzyme

4. VMD: Visual molecular dynamics

5. Molecular structure of flavocytochrome b2 at 24 Å resolution

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