Structure of the molybdenum site of Escherichia coli trimethylamine N-oxide reductase

Limei Zhang, Kimberly Johnson Nelson, K. V. Rajagopalan, Graham N. George

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

We report a structural characterization of the molybdenum site of recombinant Escherichia coli trimethylamine N-oxide (TMAO) reductase using X-ray absorption spectroscopy. The enzyme active site shows considerable similarity to that of dimethyl sulfoxide (DMSO) reductase, in that, like DMSO reductase, the TMAO reductase active site can exist in multiple forms. Examination of the published crystal structure of TMAO oxidase from Shewanella massilia indicates that the postulated Mo coordination structure is chemically impossible. The presence of multiple active site structures provides a potential explanation for the anomalous features reported from the crystal structure.

Original languageEnglish (US)
Pages (from-to)1074-1078
Number of pages5
JournalInorganic Chemistry
Volume47
Issue number3
DOIs
StatePublished - Feb 4 2008

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

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