Communication
Probing a Homoleptic PbS3 Coordination Environment in a Designed Peptide Using 207Pb NMR Spectroscopy: Implications for Understanding the Molecular Basis of Lead Toxicity†
Dr. Kosh P. Neupane,
Prof. Dr. Vincent L. Pecoraro,
Dr. Kosh P. Neupane
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-936-7628
Search for more papers by this authorProf. Dr. Vincent L. Pecoraro
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-936-7628
Search for more papers by this authorDr. Kosh P. Neupane,
Prof. Dr. Vincent L. Pecoraro,
Dr. Kosh P. Neupane
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-936-7628
Search for more papers by this authorProf. Dr. Vincent L. Pecoraro
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109 (USA), Fax: (+1) 734-936-7628
Search for more papers by this author†
V.L.P. thanks the National Institute of Health for support of this research (R01 ES0 12236).
Graphical Abstract
The lead-inhibited active site of a zinc-binding metalloenzyme in a thiol-rich coordination environment (PbS3) has been modeled by homoleptic three-strand coiled-coil peptides and characterized using natural-abundance 207Pb NMR spectroscopy (see picture: 207Pb NMR signals from two binding sites of the same protein). 207Pb NMR spectroscopy could thus be used to identify and characterize important human proteins associated with lead toxicity.
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