NDLI: Electron transfer and reaction mechanism of laccases

Content Provider	Springer Nature Link
Author	Jones, Stephen M. Solomon, Edward I.
Copyright Year	2015
Abstract	Laccases are part of the family of multicopper oxidases (MCOs), which couple the oxidation of substrates to the four electron reduction of O2 to H2O. MCOs contain a minimum of four Cu’s divided into Type 1 (T1), Type 2 (T2), and binuclear Type 3 (T3) Cu sites that are distinguished based on unique spectroscopic features. Substrate oxidation occurs near the T1, and electrons are transferred approximately 13 Å through the protein via the Cys-His pathway to the T2/T3 trinuclear copper cluster (TNC), where dioxygen reduction occurs. This review outlines the electron transfer (ET) process in laccases, and the mechanism of O2 reduction as elucidated through spectroscopic, kinetic, and computational data. Marcus theory is used to describe the relevant factors which impact ET rates including the driving force, reorganization energy, and electronic coupling matrix element. Then, the mechanism of O2 reaction is detailed with particular focus on the intermediates formed during the two 2e− reduction steps. The first 2e− step forms the peroxide intermediate, followed by the second 2e− step to form the native intermediate, which has been shown to be the catalytically relevant fully oxidized form of the enzyme.
Starting Page	869
Ending Page	883
Page Count	15
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	72
Issue Number	5
e-ISSN	14209071
Language	English
Publisher	Springer Basel
Publisher Date	2015-01-09
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Laccase Multicopper oxidase Type 1 copper Type 2 copper Type 3 copper Marcus theory Cell Biology Biomedicine general Life Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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