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• W2015594022 abstract "Qualitatively similar metal coordination as in PQQ-dependent bacterial dehydrogenases was observed for the PQQ triester in the model complex I, although the unusual five-coordinate copper(I) center is smaller and softer than the Ca2+ ion of the native enzymes. The ambidentate PQQ thus prefers coordination through the O(5)/N(6)/O(7‘) atoms even without additional support from the protein scaffold." @default.
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• W2015594022 date "1999-05-01" @default.
• W2015594022 modified "2023-09-24" @default.
• W2015594022 title "First Experimental Structure of a 1:1 Metal Complex with a PQQ Cofactor Derivative outside Dehydrogenase Enzymes" @default.
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• W2015594022 doi "https://doi.org/10.1021/ic981390h" @default.
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