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• W1701555181 endingPage "656" @default.
• W1701555181 startingPage "651" @default.
• W1701555181 abstract "Zinc/thiolate (cysteine) coordination occurs in a very large number of proteins. These coordination sites are thermodynamically quite stable. Yet the redox chemistry of thiolate ligands confers extraordinary reactivities on these sites. The significance of such ligand-centered reactions is that they affect the binding and release of zinc, thus helping to distribute zinc, and perhaps controlling zinc-dependent cellular events. One new aspect focuses on the thiolate ligands of zinc as targets for the redox action of selenium compounds. A distinctive feature of this chemistry is the capacity of selenols to catalyze the oxidation of zinc/thiolate sites. We here use a chromophoric compound, 2-nitrophenylselenocyanate, to investigate its reaction mechanism with the zinc/thiolate clusters of metallothionein, a protein that is a cellular reservoir for zinc and together with its apoprotein, thionein, is involved in zinc distribution as a zinc donor/acceptor pair. The reaction is particularly revealing as it occurs in two steps. A selenenylsulfide intermediate is formed in the fast oxidative step, followed by the generation of 2-nitrophenylselenol that initiates the second, catalytic step. The findings demonstrate the high reactivity of selenium compounds with zinc/thiolate coordination sites and the potent catalytic roles that selenoproteins and selenium redox drugs may have in affecting gene expression via modulation of the zinc content of zinc finger proteins." @default.
• W1701555181 created "2016-06-24" @default.
• W1701555181 creator A5000431856 @default.
• W1701555181 creator A5052676364 @default.
• W1701555181 date "2001-08-01" @default.
• W1701555181 modified "2023-09-23" @default.
• W1701555181 title "Catalytic Oxidation of Zinc/Sulfur Coordination Sites in Proteins by Selenium Compounds" @default.
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• W1701555181 doi "https://doi.org/10.1089/15230860152542998" @default.
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