Orientation-selected 15N-HYSCORE detection of weakly coupled nitrogens around the archaeal rieske [2Fe-2S] center.
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.
Iwasaki
Toshio
T
Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan. tiwasaki@nms.ac.jp
Kounosu
Asako
A
Uzawa
Taketoshi
T
Samoilova
Rimma I
RI
Dikanov
Sergei A
SA
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D014450:Electron Transport Complex III / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D009587:Nitrogen Isotopes; D016944:Sulfolobus / Q000737:chemistry / Q000378:metabolism
D019843:Archaeal Proteins; D007506:Iron-Sulfur Proteins; D009587:Nitrogen Isotopes; C037989:Rieske iron-sulfur protein; D014450:Electron Transport Complex III