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Probing a Homoleptic PbS 3 Coordination Environment in a Designed Peptide Using 207 Pb NMR Spectroscopy: Implications for Understanding the Molecular Basis of Lead Toxicity
Author(s) -
Neupane Kosh P.,
Pecoraro Vincent L.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201004429
Subject(s) - homoleptic , chemistry , nuclear magnetic resonance spectroscopy , spectroscopy , fluorine 19 nmr , coordination complex , two dimensional nuclear magnetic resonance spectroscopy , stereochemistry , metal , organic chemistry , physics , quantum mechanics
The lead‐inhibited active site of a zinc‐binding metalloenzyme in a thiol‐rich coordination environment (PbS 3 ) has been modeled by homoleptic three‐strand coiled‐coil peptides and characterized using natural‐abundance 207 Pb NMR spectroscopy (see picture: 207 Pb NMR signals from two binding sites of the same protein). 207 Pb NMR spectroscopy could thus be used to identify and characterize important human proteins associated with lead toxicity.