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Cysteine derivatives of the designed \u03b1\u2010helical peptides of the TRI family [Ac\u2010G\u2010(L\n                    <jats:sub>a<\/jats:sub>\n                    K\n                    <jats:sub>b<\/jats:sub>\n                    A\n                    <jats:sub>c<\/jats:sub>\n                    L\n                    <jats:sub>d<\/jats:sub>\n                    E\n                    <jats:sub>e<\/jats:sub>\n                    E\n                    <jats:sub>f<\/jats:sub>\n                    K\n                    <jats:sub>g<\/jats:sub>\n                    )\n                    <jats:sub>4<\/jats:sub>\n                    \u2010G\u2010NH\n                    <jats:sub>2<\/jats:sub>\n                    ] bind Hg\n                    <jats:sup>II<\/jats:sup>\n                    at high pH values and at peptide\/Hg\n                    <jats:sup>II<\/jats:sup>\n                    ratios of 3:1 with an unusual trigonal thiolate coordination mode. The resulting Hg\n                    <jats:sup>II<\/jats:sup>\n                    complexes are good water\u2010soluble models for Hg\n                    <jats:sup>II<\/jats:sup>\n                    binding to the protein MerR. We have carried out a parallel study using\n                    <jats:sup>199<\/jats:sup>\n                    Hg NMR and\n                    <jats:sup>199m<\/jats:sup>\n                    Hg perturbed angular correlation (PAC) spectroscopy to characterize the distinct species that are generated under different pH conditions and peptide TRI\u2005L9C\/Hg\n                    <jats:sup>II<\/jats:sup>\n                    ratios. These studies prove for the first time the formation of [Hg{(TRI\u2005L9C)\n                    <jats:sub>2<\/jats:sub>\n                    \u2010(TRI\u2005L9C\uf8ffH)}], a dithiolate\u2013Hg\n                    <jats:sup>II<\/jats:sup>\n                    complex in the hydrophobic interior of the three\u2010stranded coiled coil (TRI\u2005L9C)\n                    <jats:sub>3<\/jats:sub>\n                    .\n                    <jats:sup>199<\/jats:sup>\n                    Hg NMR and\n                    <jats:sup>199m<\/jats:sup>\n                    Hg PAC data demonstrate that this dithiolate\u2013Hg\n                    <jats:sup>II<\/jats:sup>\n                    complex is different from the dithiolate [Hg(TRI\u2005L9C)\n                    <jats:sub>2<\/jats:sub>\n                    ], and that the presence of third \u03b1\u2010helix, containing a protonated cysteine, breaks the symmetry of the coordination environment present in the complex [Hg(TRI\u2005L9C)\n                    <jats:sub>2<\/jats:sub>\n                    ]. As the pH is raised, the deprotonation of this third cysteine generates the trigonal thiolate\u2013Hg\n                    <jats:sup>II<\/jats:sup>\n                    complex Hg(TRI\u2005L9C)\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    on a timescale that is slower than the NMR timescale (0.01\u201310\u2005ms). The formation of the species [Hg{(TRI\u2005L9C)\n                    <jats:sub>2<\/jats:sub>\n                    (TRI\u2005L9C\uf8ffH)}] is the result of a compromise between the high affinity of Hg\n                    <jats:sup>II<\/jats:sup>\n                    to form dithiolate complexes and the preference of the peptide to form a three\u2010stranded coiled coil.\n                  <\/jats:p>","DOI":"10.1002\/chem.200701208","type":"journal-article","created":{"date-parts":[[2007,10,25]],"date-time":"2007-10-25T09:49:58Z","timestamp":1193305798000},"page":"9178-9190","source":"Crossref","is-referenced-by-count":69,"title":["The Application of\n                    <sup>199<\/sup>\n                    Hg NMR and\n                    <sup>199m<\/sup>\n                    Hg Perturbed Angular Correlation (PAC) Spectroscopy to Define the Biological Chemistry of Hg\n                    <sup>II<\/sup>\n                    : A Case Study with Designed Two\u2010 and Three\u2010Stranded Coiled Coils"],"prefix":"10.1002","volume":"13","author":[{"given":"Olga","family":"Iranzo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter\u2005W.","family":"Thulstrup","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seung\u2010baek","family":"Ryu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars","family":"Hemmingsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent\u2005L.","family":"Pecoraro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2007,11,8]]},"reference":[{"key":"e_1_2_7_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.41.070172.000515"},{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr030443w"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00164a080"},{"key":"e_1_2_7_4_2","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1016\/S0022-3565(24)37175-7","volume":"283","author":"Satoh M.","year":"1997","journal-title":"J. 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