Inhibition in multicopper oxidases: a critical review
Ингибирование мультикупровых оксидаз: критический обзор
2020-01-01
SCID: 54.1/c7gk9ur6
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O2-reduction catalysisbilirubin oxidaseenzyme inhibitionlaccasemulticopper oxidases
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Abstract (AI)
This review critiques the literature on inhibition of O 2 -reduction catalysis in multicopper oxidases like laccase and bilirubin oxidase and provide recommendations for best practice when carrying out experiments and interpreting published data.
Key Findings
1
It identifies issues affecting experimental studies and interpretation of inhibition data in the existing literature.
2
The review critically evaluates published research on inhibition of O2-reduction catalysis in multicopper oxidases, including laccase and bilirubin oxidase.
3
The review provides recommendations for best practices when designing inhibition experiments and interpreting published findings.
Research Object
O2-reduction catalysis in multicopper oxidases such as laccase and bilirubin oxidase
Research Subject
Inhibition mechanisms and experimental interpretation of O2-reduction catalysis
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2020-01-01
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References available in scid.ai13
Fungal laccase discovered but yet undiscovered2018
Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation2017
Two Decades of Laccases: Advancing Sustainability in the Chemical Industry2016
The Laccase Engineering Database: a classification and analysis system for laccases and related multicopper oxidases2011
Laccase: Properties and applications2009
Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences2006
Fungal laccases – occurrence and properties2006
Spectroscopic and Electronic Structure Studies of the Trinuclear Cu Cluster Active Site of the Multicopper Oxidase Laccase: Nature of Its Coordination Unsaturation2005
Substrate and Dioxygen Binding to the Endospore Coat Laccase from Bacillus subtilis2004
A Labile Regulatory Copper Ion Lies Near the T1 Copper Site in the Multicopper Oxidase CueO2003
The Protein Data Bank2000
Site-directed mutations in fungal laccase: effect on redox potential, activity and pH profile1998
Effects of Redox Potential and Hydroxide Inhibition on the pH Activity Profile of Fungal Laccases1997