Probing a Homoleptic PbS₃ Coordination Environment in a Designed Peptide Using ²⁰⁷Pb NMR Spectroscopy: Implications for Understanding the Molecular Basis of Lead Toxicity
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 t...
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Veröffentlicht in: | Angewandte Chemie (International ed.) 2010-10, Vol.49 (44), p.8177-8180 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201004429 |