title: Hyperfine Sublevel Correlation Spectroscopy Studies of Iron-Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum.
abstract: The magnetic properties of the Rieske protein purified from Chlorobaculum tepidum were investigated using electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy (HYSCORE). The g-values of the Fe2S2center were gx= 1.81, gy= 1.90, and gz= 2.03. Four classes of nitrogen signals were obtained by HYSCORE. Nitrogens 1 and 2 had relatively strong magnetic hyperfine couplings and were assigned as the nitrogen directly ligated to Fe. Nitrogens 3 and 4 had relatively weak magnetic hyperfine couplings and were assigned as the other nitrogen of the His ligands and peptide nitrogen connected to the sulfur atom via hydrogen bonding, respectively. The anisotropy of nitrogen 3 reflects the different spin density distributions on the His ligands, which influences the electron transfer to quinone.
authors.affiliation: Division of Material Science, Graduate School of Science, Nagoya University , Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8602, Japan.
authors.forename: Hiroki
authors.initials: H
authors.lastname: Nagashima
authors.affiliation: Department of Biological Sciences, Graduate School of Science, Osaka University , Toyanaka, Osaka 560-0043, Japan.
authors.forename: Hiraku
authors.initials: H
authors.lastname: Kishimoto
authors.affiliation: Institute for Protein Research, Osaka University , Suita, Osaka 565-0871, Japan.
authors.forename: Risa
authors.initials: R
authors.lastname: Mutoh
authors.affiliation: Division of Material Science, Graduate School of Science, Nagoya University , Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8602, Japan.
authors.forename: Naotaka
authors.initials: N
authors.lastname: Terashima
authors.affiliation: Department of Biological Sciences, Graduate School of Science, Osaka University , Toyanaka, Osaka 560-0043, Japan.
authors.forename: Hirozo
authors.initials: H
authors.lastname: Oh-Oka
authors.affiliation: Department of Biological Sciences, Graduate School of Science, Osaka University , Toyanaka, Osaka 560-0043, Japan.|Institute for Protein Research, Osaka University , Suita, Osaka 565-0871, Japan.
authors.forename: Genji
authors.initials: G
authors.lastname: Kurisu
authors.affiliation: Division of Material Science, Graduate School of Science, Nagoya University , Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8602, Japan.
authors.forename: Hiroyuki
authors.identifier: 0000-0003-4040-8732
authors.initials: H
authors.lastname: Mino
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D016227:Benzoquinones / Q000737:chemistry; D019414:Chlorobi / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D014450:Electron Transport Complex III / Q000737:chemistry*; D004583:Electrons; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D009584:Nitrogen / Q000737:chemistry; D013455:Sulfur / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D016227:Benzoquinones; D008024:Ligands; C037989:Rieske iron-sulfur protein; C004532:quinone; D013455:Sulfur; D007501:Iron; D014450:Electron Transport Complex III; D009584:Nitrogen