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2 Publications

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    10/19/15 | Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.
    Tebo AG, Hemmingsen L, Pecoraro VL
    Metallomics. 10/2015;7:1555 – 1561. doi: 10.1039/c5mt00228a

    Members of the ArsR/SmtB family of transcriptional repressors, such as CadC, regulate the intracellular levels of heavy metals like Cd(II), Hg(II), and Pb(II). These metal sensing proteins bind their target metals with high specificity and affinity, however, a lack of structural information about these proteins makes defining the coordination sphere of the target metal difficult. Lingering questions as to the identity of Cd(II) coordination in CadC are addressed via protein design techniques. Two designed peptides with tetrathiolate metal binding sites were prepared and characterized, revealing fast exchange between CdS3O and CdS4 coordination spheres. Correlation of (111m)Cd PAC spectroscopy and (113)Cd NMR spectroscopy suggests that Cd(II) coordinated to CadC is in fast exchange between CdS3O and CdS4 forms, which may provide a mechanism for rapid sensing of heavy metal contaminants by this regulatory protein.

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    01/08/15 | Artificial metalloenzymes derived from three-helix bundles.
    Tebo AG, Pecoraro VL
    Current Opinion in Chemical Biology. 01/2015;25C:65 – 70. doi: 10.1016/j.cbpa.2014.12.034

    Three-helix bundles and coiled-coil motifs are well-established de novo designed scaffolds that have been investigated for their metal-binding and catalytic properties. Satisfaction of the primary coordination sphere for a given metal is sufficient to introduce catalytic activity and a given structure may catalyze different reactions dependent on the identity of the incorporated metal. Here we describe recent contributions in the de novo design of metalloenzymes based on three-helix bundles and coiled-coil motifs, focusing on non-heme systems for hydrolytic and redox chemistry.

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