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铁硫蛋白模型化合物的研究进展
引用本文:孙为银,刘红科.铁硫蛋白模型化合物的研究进展[J].无机化学学报,1998,14(1):20-28.
作者姓名:孙为银  刘红科
作者单位:南京大学配位化学国家重点实验室,配位化学研究所, 南京 210093,南京大学配位化学国家重点实验室,配位化学研究所, 南京 210093
摘    要:本文综述了目前国际上对铁硫蛋白模型化合物研究的进展情况,介绍了NH---S氢键和芳香环在这些模型化合物及其天然蛋白中的作用。作为铁硫蛋白活性中心的模型,至今已有许多化合物被合成出来,通过这些模型化合物的研究知道,NH---S氢键和芳香环在调控配合物及天然蛋白的氧化还原电位和稳定性方面起着非常重要的作用。另外,作为顺式乌头酸酶、固氮酶等金属酶的模型,已成功地合成了含3Fe4S核以及含钼的铁硫簇合物。

关 键 词:铁硫蛋白  模型化合物  NH---S氢键  芳香环

PROGRESS IN THE MODEL COMPOUNDS OF IRON-SULFUR PROTEINS
Sun Weiyin and Liu Hongke.PROGRESS IN THE MODEL COMPOUNDS OF IRON-SULFUR PROTEINS[J].Chinese Journal of Inorganic Chemistry,1998,14(1):20-28.
Authors:Sun Weiyin and Liu Hongke
Institution:State Key Laboratory of Coordination Chemistry, Coordination Chemistry Institute of Nanjing University, Nanjing 210093 and State Key Laboratory of Coordination Chemistry, Coordination Chemistry Institute of Nanjing University, Nanjing 210093
Abstract:The review gives the recent progress in the model compounds of iron-sulfur proteins, and described the role of NH---S hydrogen bonds and the aromatic ring in such model complexes and in the native proteins. Up to now, as model of the active site of iron-sulfur proteins many complexes with simple alkane-, arenethiolate and cysteine-containing oligo-peptide ligands have been synthesized. From such model studies, it becomes clear theat the NH---S hydrogen bonds and aromatic ring play very important role in controlling the redox potential and stability of model complexes as well as the native proteins. In addition, the 3Fe4S cluster and molybdenum-containing iron-sulfur clusters were synthesized as model of the enzymes of aconitase, nitrogenase etc..
Keywords:iron-sulfur protein      model compounds      NH---S hydrogen bond      aromatic ring
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