Structural and functional analogue of the active site of polysulfide reductase from Wolinella succinogenes.
Structural and functional analogue of the active site of polysulfide reductase from Wolinella succinogenes.
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来自 Wolinella succinogenes 的多硫化物还原酶活性位点的结构和功能类似物。
DOI：
10.1021/ic049665i
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Sarkar,Sabyasachi
中科院分区：
文献类型：
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作者：
Nagarajan,Kowliki;Joshi,HemantK;Chaudhury,PradeepK;Pal,Kuntal;Cooney,JJonA;Enemark,JohnH;Sarkar,Sabyasachi
从 [PPh4]2[MoO(S2C2(CN)2)2] (1) 合成 [PPh4]2[Mo(SPh)2(S2C2(CN)2)2] (2) 已实现模拟具有两个硫醇盐和两个双(烯-二硫醇盐)配体的多硫化物还原酶假定的 {Mo(S)6} 核心。化合物 2 与多硫化物反应生成 H2S，模拟多硫化物还原酶的功能。在潮湿溶剂中，2 容易转化为 1，这表明在适当的疏水/亲水条件下，DMSO 还原酶类酶中可能会发生 {MoIVO} 和 {MoIV−X} (X = O−Ser, S−Cys, Se−Cys) 部分的相互转化。
Synthesis of [PPh4]2[Mo(SPh)2(S2C2(CN)2)2] (2) from [PPh4]2[MoO(S2C2(CN)2)2] (1) has been achieved to mimic the postulated {Mo(S)6} core of polysulfide reductase with two thiolates and two bis(ene-dithiolate) ligands. Compound2reacts with polysulfide to yield H2S, modeling the function of polysulfide reductase. The facile conversion of2back to1in moist solvent suggests that the interconversion of the {MoIVO} and {MoIV−X} (X = O−Ser, S−Cys, Se−Cys) moieties might occur in the DMSO reductase class of enzymes under appropriate hydrophobic/hydrophilic conditions.