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-Reference-Cited by-同舟云学术

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

Published:2016-05-25 Issue:6 Volume:13 Page:798-806
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 Lucca I-55100

Publisher

Wiley

Subject

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

Reference32 articles.

1. Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme-Substrate-Dioxygen Configuration in a Cofactor-free Oxidase

2. Evolutionary history and metabolic insights of ancient mammalian uricases

3. Crystal structure of Bacillus fastidious uricase reveals an unexpected folding of the C-terminus residues crucial for thermostability under physiological conditions

4. The Neutron Structure of Urate Oxidase Resolves a Long-Standing Mechanistic Conundrum and Reveals Unexpected Changes in Protonation

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