On Dioxygen Permeation through a Dehydrogenase-Pyrroloquinoline Quinone Complex. A Molecular-Dynamics Investigation
Author:
Publisher
Wiley
Subject
Molecular Biology,Molecular Medicine,General Chemistry,Biochemistry,General Medicine,Bioengineering
Reference23 articles.
1. Existence of a novel prosthetic group, PQQ, in mebrane-bound, electron transport chain-linked, primary dehydrogenases of oxidative bacteria
2. Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone
3. Multistep, Eight-Electron Oxidation Catalyzed by the Cofactorless Oxidase, PqqC: Identification of Chemical Intermediates and Their Dependence on Molecular Oxygen
4. On the Egress of Carbon Monoxide from Myoglobin
5. Understanding How H-NOX (Heme Nitric Oxide/Oxygen) Domain Works Needs First Clarifying How Diatomic Gases Are Relocated Inside This Sensing Protein. A Molecular-Mechanics Approach
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1. On the Permeation by Dioxygen of Urate Oxidase fromAspergillus flavusin Complex with Xanthine Anion: Dioxygen Pathways and a Portrait of the Enzyme Cavities from Molecular Dynamics Simulations in Water Solution;Chemistry & Biodiversity;2016-05-25
2. 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;Chemistry & Biodiversity;2014-06
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