The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen

Tran Chin Yang, Nathan K. Maeser, Mikhail Laryukhin, Hong In Lee, Dennis R. Dean*, Lance C. Seefeldt, Brian M. Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticle

69 Scopus citations

Abstract

X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe7S9:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either 14N or 15N as the exclusive N source. All of the 14N or 15N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N.

Original languageEnglish (US)
Pages (from-to)12804-12805
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number37
DOIs
StatePublished - Sep 21 2005

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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