Hyperfine Sublevel Correlation Spectroscopy Studies of Iron-Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum
Hyperfine Sublevel Correlation Spectroscopy Studies of Iron-Sulfur Cluster in Rieske Protein from Green Sulfur Bacterium Chlorobaculum tepidum
复制标题
绿硫杆菌温热绿杆菌Rieske蛋白中铁硫簇的超精细亚能谱研究
DOI：
10.1021/acs.jpcb.6b12968
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Hiroyuki Mino
中科院分区：
文献类型：
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作者：
Hiroki Nagashima;Hiraku Kishimoto;Risa Mutton;Naotaka Terashima;Hirozo Oh-Oka;Genji Kurisu;Hiroyuki Mino
利用电子顺磁共振和超精细次能级相关谱（HYSCORE）研究了从高温绿杆菌（Chlorobaculum tepidum）中纯化的Rieske蛋白的磁性。Fe_2S_2心的g值为：x = 1.81，gy = 1.90，gz = 2.03。HYSCORE获得了四类氮信号。氮原子1和2具有相对较强的磁性超精细耦合，并被指定为直接连接到Fe的氮原子。氮3和4具有相对较弱的磁性超精细耦合，并分别被指定为His配体的其他氮和通过氢键与硫原子连接的肽氮。氮3的各向异性反映了His配体上不同的自旋密度分布，这影响了电子向醌的转移。
The magnetic properties of the Rieske protein purified fromChlorobaculum tepidumwere investigated using electron paramagnetic resonance and hyperfine sublevel correlation spectroscopy (HYSCORE). Theg-values of the Fe2S2center weregx= 1.81,gy= 1.90, andgz= 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.