Related ArticlesMercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex.
Science. 1995 Apr 21;268(5209):380-5
Authors: Utschig LM, Bryson JW, O'Halloran TV
Structural insights have been provided by mercury-199 nuclear magnetic resonance (NMR) into the metal receptor site of the MerR metalloregulatory protein alone and in a complex with the regulatory target, DNA. The one- and two-dimensional NMR data are consistent with a trigonal planar Hg-thiolate coordination environment consisting only of Cys side chains and resolve structural aspects of both metal ion recognition and the allosteric mechanism. These studies establish 199Hg NMR techniques as useful probes of the metal coordination environment of regulatory proteins, copper enzymes, and zinc transcription factor complexes as large as 50 kilodaltons.
[Stan NMR blog] Mercury in-vivo imaging?
Mercury in-vivo imaging?
Answer to a query about the feasibility of 199Hg MRI
Source: Stan blog library
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Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex.
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