Two-dimensional pulsed electron spin resonance characterization of 15N-labeled archaeal Rieske-type ferredoxin.
Two-dimensional electron spin-echo envelope modulation (ESEEM) analysis of the uniformly (15)N-labeled archaeal Rieske-type [2Fe-2S] ferredoxin (ARF) from Sulfolobus solfataricus P1 has been conducted in comparison with the previously characterized high-potential protein homologs. Major differences among these proteins were found in the hyperfine sublevel correlation (HYSCORE) lineshapes and intensities of the signals in the (++) quadrant, which are contributed from weakly coupled (non-coordinated) peptide nitrogens near the reduced clusters. They are less pronounced in the HYSCORE spectra of ARF than those of the high-potential protein homologs, and may account for the tuning of Rieske-type clusters in various redox systems.
Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Tokyo 113-8602, Japan. tiwasaki@nms.ac.jp
Toshio
T
Iwasaki
Rimma I
RI
Samoilova
Asako
A
Kounosu
Sergei A
SA
Dikanov
D019843:Archaeal Proteins / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D014450:Electron Transport Complex III / Q000737:chemistry*; D005288:Ferredoxins / Q000737:chemistry*; D007553:Isotope Labeling; D009587:Nitrogen Isotopes; D048229:Sulfolobus solfataricus
D019843:Archaeal Proteins; D005288:Ferredoxins; D009587:Nitrogen Isotopes; C037989:Rieske iron-sulfur protein; D014450:Electron Transport Complex III