Orientation-selected 15N-HYSCORE detection of weakly coupled nitrogens around the archaeal rieske [2Fe-2S] center

J Am Chem Soc. 2004 Nov 3;126(43):13902-3. doi: 10.1021/ja045898x.


The weakly coupled 15N atoms around a reduced Rieske [2Fe-2S] cluster of the uniformly 15N-labeled, hyperthermostable archaeal Rieske protein appear to produce readily observable cross-peaks in the HYSCORE spectra, with the well-resolved couplings of 0.3-0.4 MHz for the Nepsilon and 1.1 MHz for the peptide backbone nitrogens, in addition to the contributions from the coordinated Ndelta atoms. These features can be used for structure-mechanism studies of the biological redox protein system involving the weakly coupled nitrogens in coupled electron-proton transfer reactions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism
  • Electron Spin Resonance Spectroscopy / methods
  • Electron Transport Complex III / chemistry*
  • Electron Transport Complex III / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism
  • Nitrogen Isotopes
  • Sulfolobus / chemistry
  • Sulfolobus / metabolism


  • Archaeal Proteins
  • Iron-Sulfur Proteins
  • Nitrogen Isotopes
  • Rieske iron-sulfur protein
  • Electron Transport Complex III