首页> 外文会议>Asia Pacific Electron Paramagnetic Resonance/Electron Spin Resonance Symposium >The 2Fe-2S cluster in sulredoxin from the thermoacidophilic archaeon sulfolobus tokodaii strain 7,a novel water-soluble Rieske protein
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The 2Fe-2S cluster in sulredoxin from the thermoacidophilic archaeon sulfolobus tokodaii strain 7,a novel water-soluble Rieske protein

机译:来自热酸碱酸古素磺脲类Tokodaii菌株7的2Fe-2S簇中的硫酸辛菌,一种新型水溶性Rieske蛋白质

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摘要

The [2Fe-2S] cluster surrounding in reduced sulredoxin from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7 was examined by one- and two-dimensional electron spin echo envelope modulation (ESEEM) spectroscopy. ESEEM spectra revealed two coordinated nitrogens assigned to two histidine ligands and the lines from several non-exchangeable protons. No strongly coupled protons involved in hydrogen bonds near the reduced Rieske center were detected. These results are discussed in light of the structural, redox and spectroscopic characteristics of this ubiquitous electron transfer protein family.
机译:通过单一和二维电子旋转回波包络(ESEEM)光谱检查来自热酸碱酸古氏磺脲菌菌菌菌菌菌菌株7中的[2FE-2S]簇。 Eseem光谱揭示了两种分配给两个组织配体的两个协调氮,来自几种不可交换质子的萘。检测到涉及减少的Rieske中心附近涉及氢键的强耦合质子。鉴于这种普遍存在的电子转移蛋白家族的结构,氧化还原和光谱特征,讨论了这些结果。

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