Structural characterization of the binding site in the merr metalloregulatory protein

Kimber Clark, James E. Penner-Hahn, Lisa Utschig, Thomas V. O'halloran

Research output: Contribution to journalArticlepeer-review

Abstract

The Zinc and Cadmium forms of MerR, a metalloregulatory protein involved in bacterial mercury detoxification, have been studied using X-ray absorption spectroscopy. Previous work has shown the Hg-MeiR to have a unique three coordinate HgS3 environment. Preliminary analysis of the EXAFS data for the Cd- and Zn-MerR derivatives suggests a higher coordination number in these cases.

Original languageEnglish (US)
Pages (from-to)487-489
Number of pages3
JournalJapanese Journal of Applied Physics
Volume32
DOIs
StatePublished - Jan 1993

Keywords

  • DNA transcription
  • MerR
  • Metalloregulatory protein

ASJC Scopus subject areas

  • Engineering(all)
  • Physics and Astronomy(all)

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