{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":46,"searchCount":0},"additional":{"submitter":["Radford RJ"],"funding":["NIDDK NIH HHS"],"pagination":["7106-15"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2920064"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["49(15)"],"pubmed_abstract":["We report here the construction of phenanthroline (Phen) and terpyridine (Terpy)-based hybrid coordination motifs (HCMs), which were installed on the surface of the four-helical bundle hemeprotein cytochrome cb(562). The resulting constructs, termed HPhen1, HPhen2, HPhen3, and HTerpy1, feature HCMs that are composed of a histidine ligand and a Phen or Terpy functionality located two helix turns away, yielding stable tri- or tetradentate coordination platforms. Our characterization of the tridentate HCMs indicates that they accommodate many divalent metal ions (Co(2+), Ni(2+), Cu(2+), Zn(2+)) with nanomolar to femtomolar affinities, lead to significant stabilization of the alpha-helical protein scaffold through metal-mediated cross-linking, assert tight control over protein dimerization, and provide stable and high-affinity binding sites for substitution-inert metal probes. Our analyses suggest that such tridentate HCMs may be used modularly on any alpha-helical protein surface in a sequence-independent fashion."],"journal":["Inorganic chemistry"],"pubmed_title":["Modular and versatile hybrid coordination motifs on alpha-helical protein surfaces."],"pmcid":["PMC2920064"],"funding_grant_id":["T32 DK007233","T32DK007233","T32 DK007233-35"],"pubmed_authors":["Nguyen PC","Tezcan FA","Radford RJ"],"view_count":["46"],"additional_accession":[]},"is_claimable":false,"name":"Modular and versatile hybrid coordination motifs on alpha-helical protein surfaces.","description":"We report here the construction of phenanthroline (Phen) and terpyridine (Terpy)-based hybrid coordination motifs (HCMs), which were installed on the surface of the four-helical bundle hemeprotein cytochrome cb(562). The resulting constructs, termed HPhen1, HPhen2, HPhen3, and HTerpy1, feature HCMs that are composed of a histidine ligand and a Phen or Terpy functionality located two helix turns away, yielding stable tri- or tetradentate coordination platforms. Our characterization of the tridentate HCMs indicates that they accommodate many divalent metal ions (Co(2+), Ni(2+), Cu(2+), Zn(2+)) with nanomolar to femtomolar affinities, lead to significant stabilization of the alpha-helical protein scaffold through metal-mediated cross-linking, assert tight control over protein dimerization, and provide stable and high-affinity binding sites for substitution-inert metal probes. Our analyses suggest that such tridentate HCMs may be used modularly on any alpha-helical protein surface in a sequence-independent fashion.","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Aug","modification":"2024-11-13T17:30:41.33Z","creation":"2019-03-26T22:30:14Z"},"accession":"S-EPMC2920064","cross_references":{"pubmed":["20617830"],"doi":["10.1021/ic100926g"]}}