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• W2950545308 startingPage "11304" @default.
• W2950545308 abstract "High potential multicopper oxidases (MCOs) have T1 reduction potentials >600 mV (vs normal hydrogen electrode), making them important catalysts for O2 reduction in various biotechnological applications. The oxygen reduction mechanism for the low potential MCOs is well-characterized; however, O2 reactivity of high potential MCOs is not well understood. In this study, we have shown that laccase from Trametes versicolor, where the T1 redox potential is increased by ∼350 mV over that of the low potential MCOs corresponding to an 8 kcal/mol decrease in the driving force, exhibits a slower intramolecular electron transfer (IET) rate to the trinuclear Cu cluster (TNC) in the native intermediate (NI), relative to the low potential MCO from Rhus vernicifera laccase. This IET rate is, however, >102 times faster than the decay rate of the NI, demonstrating that this intermediate form of the enzyme is catalytically relevant enabling fast turnover. However, in contrast to the low potential MCOs where T1 reduction by substrate is rate limiting, the rate limiting step in turnover of high potential MCOs is the first IET to NI. Part of the reduction potential difference of the T1 sites in high vs low potential MCOs is balanced by an ∼100 mV higher reduction potential of NI due to the more positive protein environment in the vicinity of the TNC." @default.
• W2950545308 created "2019-06-27" @default.
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• W2950545308 creator A5051987123 @default.
• W2950545308 date "2019-06-19" @default.
• W2950545308 modified "2023-09-30" @default.
• W2950545308 title "O₂ Reduction to Water by High Potential Multicopper Oxidases: Contributions of the T1 Copper Site Potential and the Local Environment of the Trinuclear Copper Cluster" @default.
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• W2950545308 doi "https://doi.org/10.1021/jacs.9b05230" @default.
• W2950545308 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6662574" @default.
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• W2950545308 hasPublicationYear "2019" @default.
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