On the Permeation by Dioxygen of the Cofactor-Independent Unusual Oxygenase RhCC, in Complex with Substrate 4-Hydroxyphenylenolpyruvate. A Molecular Dynamics Investigation-Reference-Cited by-同舟云学术

On the Permeation by Dioxygen of the Cofactor-Independent Unusual Oxygenase RhCC, in Complex with Substrate 4-Hydroxyphenylenolpyruvate. A Molecular Dynamics Investigation

Published:2016-03 Issue:3 Volume:13 Page:331-335
ISSN:1612-1872
Container-title:Chemistry & Biodiversity
language:en
Short-container-title:Chem. Biodiversity

Author:

Pietra Francesco¹

Affiliation:

1. Accademia Lucchese di Scienze, Lettere e Arti, Classe di Scienze; Palazzo Ducale; IT-55100 Lucca Italy

Publisher

Wiley

Subject

Molecular Biology,Molecular Medicine,General Chemistry,Biochemistry,General Medicine,Bioengineering

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/cbdv.201500211/fullpdf

Reference20 articles.

1. On the Egress of Carbon Monoxide from Myoglobin

2. On the Pathways for CO Egress from Carboxy Human Cytoglobin. A Molecular-Dynamics Investigation

3. Binding Pockets and Pathways for Dioxygen through the KijD3N-Oxygenase in Complex with Flavin Mononucleotide Cofactor and a 3-Aminoglucose Substrate: Predictions from Molecular Dynamics Simulations

4. Binding Pockets and Permeation Channels for Dioxygen through Cofactorless 3-Hydroxy-2-methylquinolin-4-one 2,4-Dioxygenase in Association with Its Natural Substrate, 3-Hydroxy-2-methylquinolin-4(1H)-one. A Perspective from Molecular Dynamics Simulations

5. On the Pathways of Biologically Relevant Diatomic Gases through Proteins. Dioxygen and Heme Oxygenase from the Perspective of Molecular Dynamics

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