Radicals from One-Electron Oxidation of 4-Aminoresorcinol:  Models for the Active Site Radical Intermediate in Copper Amine Oxidases

2000 ◽  
Vol 104 (24) ◽  
pp. 5832-5839 ◽  
Author(s):  
Roger H. Bisby ◽  
Steven A. Johnson ◽  
Anthony W. Parker
Keyword(s):  
Active Site ◽  
Amine Oxidases ◽  
Radical Intermediate ◽  
Copper Amine Oxidases ◽  
Copper Amine

scholarly journals Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38631-38639
Author(s):  
Mitsuo Shoji ◽  
Takeshi Murakawa ◽  
Mauro Boero ◽  
Yasuteru Shigeta ◽  
Hideyuki Hayashi ◽  
...  
Keyword(s):  
Biogenic Amines ◽  
Active Site ◽  
Amine Oxidase ◽  
First Principle ◽  
Amine Oxidases ◽  
Oxidative Deamination ◽  
Copper Amine Oxidase ◽  
First Principle Calculations ◽  
Copper Amine Oxidases ◽  
Copper Amine

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

scholarly journals Time-Resolved Resonance Raman Studies of Radicals From 4-Aminoresorcinol as Models for the Active Site Radical Intermediate in Copper Amine Oxidases

1999 ◽  
Vol 19 (1-4) ◽  
pp. 201-208 ◽  
Author(s):  
Roger H. Bisby ◽  
Steven A. Johnson ◽  
Anthony W. Parker ◽  
Susan M. Tavender
Keyword(s):  
Active Site ◽  
Resonance Raman ◽  
Amine Oxidases ◽  
Deprotonated Form ◽  
Radical Intermediate ◽  
Time Resolved ◽  
Free Radical Intermediate ◽  
Stable Product ◽  
Resonance Raman Spectra ◽  
Copper Amine Oxidases

Radicals formed by one-electron oxidation of 4-aminoresorcinol have been studied as models for the active site free radical intermediate which forms as a stable product during anaerobic incubation of amine oxidases with amine substrates. Pulse radiolysis shows that the radical undergoes ionisations with pKa's of 3.4 and 6.4. Although the two deprotonated forms are difficult to distinguish by absorption spectroscopy, they have clearly different resonance Raman spectra. Comparison with the resonance Raman spectrum of the enzyme intermediate shows it to be the singly deprotonated form of the radical.

scholarly journals Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases.

1992 ◽  
Vol 267 (12) ◽  
pp. 7979-7982
Author(s):  
D Mu ◽  
S.M. Janes ◽  
A.J. Smith ◽  
D.E. Brown ◽  
D.M. Dooley ◽  
...  
Keyword(s):  
Active Site ◽  
Amine Oxidases ◽  
Topa Quinone ◽  
Copper Amine Oxidases ◽  
Copper Amine

The active site of copper amine oxidases

1984 ◽  
Vol 23 (2-3) ◽  
pp. 325-330 ◽  
Author(s):  
Bruno Mondoví ◽  
Stefania Sabatini ◽  
Olivia Befani
Keyword(s):  
Active Site ◽  
Amine Oxidases ◽  
Copper Amine Oxidases ◽  
Copper Amine

ChemInform Abstract: The Reductive and Oxidative Half-Reactions and the Role of Copper Ions in Plant and Mammalian Copper-Amine Oxidases.

ChemInform ◽  
2001 ◽  
Vol 32 (11) ◽  
pp. no-no
Author(s):  
Alessandra Padiglia ◽  
Rosaria Medda ◽  
Andrea Bellelli ◽  
Enzo Agostinelli ◽  
Laura Morpurgo ◽  
...  
Keyword(s):  
Copper Ions ◽  
Amine Oxidases ◽  
Copper Amine Oxidases ◽  
Copper Amine

Design, synthesis and evaluation of mechanism-based inhibitors of copper amine oxidases

1994 ◽  
pp. 259-261 ◽  
Author(s):  
Lawrence M. Sayre ◽  
Fengjiang Wang ◽  
Younghee Lee ◽  
He Huang ◽  
Frederick T. Greenaway ◽  
...  
Keyword(s):  
Amine Oxidases ◽  
Design Synthesis ◽  
Copper Amine Oxidases ◽  
Copper Amine
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