Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex

Lisa M. Utschig*, James W. Bryson, Thomas V. O'Halloran

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

146 Scopus citations


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 aliosteric 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.

Original languageEnglish (US)
Pages (from-to)380-385
Number of pages6
Issue number5209
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • General


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