caa a22 4500 606176829 CHVBK 20210128100749.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00018-014-1826-6 doi (NATIONALLICENCE)springer-10.1007/s00018-014-1826-6 Electron transfer and reaction mechanism of laccases [Elektronische Daten] [Stephen Jones, Edward Solomon] 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 13Å 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. Springer Basel, 2015 Laccase nationallicence Multicopper oxidase nationallicence Type 1 copper nationallicence Type 2 copper nationallicence Type 3 copper nationallicence Marcus theory nationallicence Jones Stephen Department of Chemistry, Stanford University, 333 Campus Drive, 94305, Stanford, CA, USA aut Solomon Edward Department of Chemistry, Stanford University, 333 Campus Drive, 94305, Stanford, CA, USA aut Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 869-883 1420-682X 72:5<869 2015 72 18 https://doi.org/10.1007/s00018-014-1826-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1826-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jones Stephen Department of Chemistry, Stanford University, 333 Campus Drive, 94305, Stanford, CA, USA aut NATIONALLICENCE 700 1- Solomon Edward Department of Chemistry, Stanford University, 333 Campus Drive, 94305, Stanford, CA, USA aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 869-883 1420-682X 72:5<869 2015 72 18