Two-dimensional pulsed electron spin resonance characterization of 15N-labeled archaeal Rieske-type ferredoxin

• Published in: FEBS letters Vol. 583; no. 21; pp. 3467 - 3472
• Main Authors: Iwasaki, Toshio, Samoilova, Rimma I., Kounosu, Asako, Dikanov, Sergei A.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03-11-2009
• Subjects: [2Fe–2S] cluster; Archaea; Archaeal Proteins - chemistry; archaeal Rieske-type ferredoxin from Sulfolobus solfataricus; ARF; E m; Electron paramagnetic resonance; Electron Spin Resonance Spectroscopy; Electron spin-echo envelope modulation; Electron Transport Complex III - chemistry; electron-nuclear double resonance; ENDOR; EPR; ESEEM; Ferredoxin; Ferredoxins - chemistry; Fourier transform; hyperfine; Hyperfine sublevel correlation; HYSCORE; Isotope Labeling; Nitrogen Isotopes; NMR; nuclear magnetic resonance; peptide backbone nitrogen; redox potential; Rieske; Rieske-type ferredoxin component of toluene 4-monooxygenase complex; SDX; Sulfolobus solfataricus; sulredoxin (a high-potential Rieske protein from Sulfolobus tokodaii); T4moC; EPR; SDX; Archaea; [2Fe–2S] cluster; ESEEM; ENDOR; FT; HYSCORE; NMR; Hyperfine sublevel correlation; E m; ARF; Electron spin-echo envelope modulation; T4moC; Electron paramagnetic resonance; Rieske; Ferredoxin; HF; N p
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2009.09.050

Two-dimensional electron spin-echo envelope modulation (ESEEM) analysis of the uniformly
15N-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.