A substrate-cofactor free radical intermediate in the reaction mechanism of copper amine oxidase

Biochemistry ◽  
1992 ◽  
Vol 31 (1) ◽  
pp. 8-12 ◽  
Author(s):  
Jens Z. Pedersen ◽  
Said El-Sherbini ◽  
Alessandro Finazzi-Agro ◽  
Giuseppe Rotilio
Keyword(s):  
Free Radical ◽  
Reaction Mechanism ◽  
Amine Oxidase ◽  
Radical Intermediate ◽  
Copper Amine Oxidase ◽  
Free Radical Intermediate ◽  
Copper Amine

The reaction mechanism of copper amine oxidase: detection of intermediates by the use of substrates and inhibitors

Biochemistry ◽  
1995 ◽  
Vol 34 (50) ◽  
pp. 16375-16381 ◽  
Author(s):  
Rosaria Medda ◽  
Alessandra Padiglia ◽  
Jens Z. Pedersen ◽  
Giuseppe Rotilio ◽  
Alessandro Finazzi Agro ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Copper Amine

Photochemical decomposition of t-butyl hydroperoxide; Photocatalytical effects of VO(II) and Co(III) 2,4-pentanedionates

1988 ◽  
Vol 53 (3) ◽  
pp. 497-505 ◽  
Author(s):  
Stanislav Luňák ◽  
Aleksandr I. Kokorin ◽  
Eva Mácová ◽  
Pavel Lederer
Keyword(s):  
Free Radical ◽  
Opposite Effect ◽  
Radical Intermediate ◽  
Butyl Hydroperoxide ◽  
Free Radical Intermediate ◽  
Catalytically Active ◽  
Photochemical Decomposition ◽  
Epr Signal

It has been found that [VO(acac)2] and [Co(acac)3] increase the rate of t-BuOOH photolysis, whereas [Fe(acac)3] has the opposite effect. Redox changes of the catalytically active [VO(acac)2] were followed using the EPR technique. An EPR signal from a free radical intermediate of photochemical decomposition of t-BuOOH was recorded, and the concentration of the intermediate was monitored during the reaction.

scholarly journals Time-resolved analysis of catalytic reaction of copper amine oxidase fromArthrobacter globiformis

2011 ◽  
Vol 67 (a1) ◽  
pp. C225-C225
Author(s):  
H. Yamaguchi ◽  
M. Kataoka ◽  
H. Oya ◽  
A. Tominaga ◽  
M. Ohtsu ◽  
...  
Keyword(s):  
Catalytic Reaction ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Time Resolved ◽  
Copper Amine

Molecular cloning and characterization of copper amine oxidase from Huperzia serrata

2012 ◽  
Vol 22 (18) ◽  
pp. 5784-5790 ◽  
Author(s):  
Jieyin Sun ◽  
Hiroyuki Morita ◽  
Guoshen Chen ◽  
Hiroshi Noguchi ◽  
Ikuro Abe
Keyword(s):  
Molecular Cloning ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Huperzia Serrata ◽  
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.

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