Given the similarities in coordination properties between multiple transition metals, metal ion substitution is likely to contribute to metal ion toxicity and/or normal regulatory function. For example, it has been proposed that the zinc finger (ZF)-based Sp1 transcription factor serves as a regulator of multiple copper-binding proteins in response to copper level variations in mammalian cells. In this context, we present spectroscopic studies on multiple ZF peptides, including those based upon the Sp1 ZF domains, aimed at characterizing the resulting copper-bound species formed upon addition of Cu(I) to apo- and metal-reconstituted peptides. Efforts to examine the impact of Cu(I) on the DNA binding properties of Sp1 are also presented.<br/>

Copper (I) substitution at zinc (II) binding domains: Characterization of speciation and functional studies

253rd National Meeting (2017)

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