STRUCTURE AND PROPERTIES OF A SYNTHETIC ANALOG OF BACTERIAL IRON-SULFUR PROTEINS
STRUCTURE AND PROPERTIES OF A SYNTHETIC ANALOG OF BACTERIAL IRON-SULFUR PROTEINS
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DOI：
10.1073/pnas.69.9.2437
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发表时间：
1972-01-01
影响因子：
11.1
通讯作者：
PHILLIPS, WD
中科院分区：
文献类型：
--
作者：
HERSKOVITZ, T;HOLM, RH;PHILLIPS, WD
合成了（Et_4N）_2 [Fe_4S_4（SCH_2Ph）_4]，用X射线衍射法测定了其结构。该阴离子的Fe_4S_4核心具有D_2d对称性构型，与产气微球菌（Micrococcus aerogenes）铁氧还蛋白和铬菌（Chromatium）高电位铁蛋白的Fe_4S_4活性中心结构密切相关。四聚阴离子的电子性质已经部分通过测量质子磁共振，穆斯堡尔，光电子和电子光谱，和磁化率来表征。[Fe 4S 4（SCH 2 Ph）4]2-和蛋白质的相应性质的比较意味着合成的四聚体、还原形式的高电位蛋白质和氧化形式的8-Fe铁氧化还原蛋白的氧化水平是等同的。四聚体具有与铁氧化还原蛋白的4-Fe中心相关的单电子氧化还原能力。[Fe 4S 4（SCH 2 Ph）4]2-的结构和集体电子特征表明它是第一个明确定义的铁硫蛋白活性位点的合成类似物。
The compound (Et4N)2[Fe4S4(SCH2Ph)4] has been prepared and its structure determined by x-ray diffraction. The Fe4S4core of the anion possesses a configuration of D2dsymmetry that is closely related to the Fe4S4active-site structures of the high-potential iron protein fromChromatiumand the ferredoxin fromMicrococcus aerogenes. Electronic properties of the tetrameric anion have been partially characterized by measurement of proton magnetic resonance, Mössbauer, photoelectron, and electronic spectra, and magnetic susceptibility. Comparison of corresponding properties of [Fe4S4(SCH2Ph)4]2-and the proteins implies that the oxidation levels of the synthetic tetramer, the reduced form of the high-potential protein, and the oxidized form of the 8-Fe ferredoxins are equivalent. The tetramer possesses the one-electron redox capacity associated with the 4-Fe centers of the ferredoxins. The structural and collective electronic features of [Fe4S4(SCH2Ph)4]2-reveal it to be the first well-defined synthetic analogue of the active site of an iron-sulfur protein.