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• W2323354385 abstract "The multicopper oxidases (MCOs) are the family of enzymes that catalyze the 4-electron reduction of O2 to H2O coupled to the four 1-electron oxidations of substrate. In the catalytic cycle electrons are transferred intramolecularly over ∼13 Å from a Type 1 (T1) Cu site that accepts electrons from substrate to a trinuclear Cu cluster (TNC) where O2 is reduced to H2O at rapid rates consistent with turnover (560 s(-1)). The oxygen reduction mechanism for the MCOs is well-characterized, whereas the rereduction is less understood. Our initial study of Rhus vernicifera Laccase (Heppner et al. J. Am. Chem. Soc. 2013, 135, 12212) experimentally established that the native intermediate (NI), the species formed upon O-O bond cleavage, is reduced with an IET rate >700 s(-1) and is the catalytically relevant fully oxidized form of the enzyme, rather than the resting state. In this report, we present kinetic and spectroscopic results coupled to DFT calculations that evaluate the mechanism of the 3 e(-)/3 H(+) reduction of NI, where all three catalytically relevant intramolecular electron transfer (IET) steps are rapid and involve three different structural changes. These three rapid IET processes reflect the sophisticated mechanistic control of the TNC to enable rapid turnover. All three IET processes are fast due to the associated protonation of the bridging oxo and hydroxo ligands, generated by O-O cleavage, to form water products that are extruded from the TNC upon full reduction, thereby defining a unifying mechanism for oxygen reduction and rapid IET by the TNC in the catalytic cycle of the MCOs." @default.
• W2323354385 created "2016-06-24" @default.
• W2323354385 creator A5018944651 @default.
• W2323354385 creator A5024342453 @default.
• W2323354385 creator A5037572396 @default.
• W2323354385 date "2014-12-09" @default.
• W2323354385 modified "2023-10-16" @default.
• W2323354385 title "Mechanism of the Reduction of the Native Intermediate in the Multicopper Oxidases: Insights into Rapid Intramolecular Electron Transfer in Turnover" @default.
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• W2323354385 doi "https://doi.org/10.1021/ja509150j" @default.
• W2323354385 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4291763" @default.
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• W2323354385 hasPublicationYear "2014" @default.
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