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• W1994313247 abstract "Copper complexes with cysteine have been investigated by optical spectroscopy, NMR and ESR. Cuprous ions strongly bind to the thiol group of Cys forming polymeric species with bridging thiolate sulfur according to a stoichiometry of about 1:1.2 and stability constant of the order of 1010 M−1. Cupric ions in the presence of cysteine, up to a ratio 0.45:1, are reduced to Cu(I) with stoichiometric production of cystine. The Cu(I) produced by this reaction is complexed by the excess of Cys. Trace amounts of Cu(II) exceeding the ratio 0.45:1 induce fast and complete oxidation of the Cys–Cu(I) complex to cystine with concomitant production of Cu(0) which precipitates. The experimental data are consistent with a mechanism by which Cu(II) oxidizes the complex Cys–Cu(I) to cystine producing aqueous Cu(I) which undergoes dismutation regenerating Cu(II). According to this mechanism the uncomplexed Cu(II) plays a catalytic oxidative role in the absence of molecular oxygen. The biological significance of these reactions is discussed." @default.
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• W1994313247 date "2004-09-01" @default.
• W1994313247 modified "2023-10-14" @default.
• W1994313247 title "Interaction of copper with cysteine: stability of cuprous complexes and catalytic role of cupric ions in anaerobic thiol oxidation" @default.
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• W1994313247 doi "https://doi.org/10.1016/j.jinorgbio.2004.06.008" @default.
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