Zinc thiolate reactivity toward nitrogen oxides: insights into the interaction of Zn2+ with S-nitrosothiols and implications for nitric oxide synthase.
Zinc thiolate reactivity toward nitrogen oxides: insights into the interaction of Zn2+ with S-nitrosothiols and implications for nitric oxide synthase.
复制标题
DOI：
10.1021/ic3007684
复制
发表时间：
2012-07-02
影响因子：
4.6
通讯作者：
Lippard SJ
中科院分区：
文献类型：
--
作者：
Kozhukh J;Lippard SJ
制备了含N2S三齿配体的硫酸锌配合物，研究了其对一氧化氮合酶（NOS）四半胱氨酸硫酸锌位点活性氮的反应性。在没有二氧的情况下，这些配合物对一氧化氮没有反应，这强烈表明一氧化氮不可能是在体内直接导致s -亚硝基硫醇形成和在一氧化氮二聚体界面上损失Zn2+的物质。然而，当硫代锌溶液暴露于有空气存在的NO或NO2或NOBF4时，确实会形成s -亚硝基硫醇，这表明这些活性氮/氧能够从酶中释放锌，可能是通过s -亚硝基硫醇的生成。简单的Zn2+盐与预形成的s -亚硝基硫醇相互作用导致-SNO部分分解，释放气态NO和N2O。讨论了这种化学的潜在生物学意义。
Zinc thiolate complexes containing N2S tridentate ligands were prepared to investigate their reactivity toward reactive nitrogen species, chemistry proposed to occur at the zinc tetracysteine thiolate site of nitric oxide synthase (NOS). The complexes are unreactive toward nitric oxide in the absence of dioxygen, strongly indicating that NO cannot be the species directly responsible for S-nitrosothiol formation and loss of Zn2+ at the NOS dimer interface in vivo. S-Nitrosothiol formation does occur upon exposure of zinc thiolate solutions to NO in the presence of air, however, or to NO2 or NOBF4, indicating that these reactive nitrogen/oxygen species are capable of liberating zinc from the enzyme, possibly through generation of the S-nitrosothiol. Interaction between simple Zn2+ salts and pre-formed S-nitrosothiols leads to decomposition of the –SNO moiety, resulting in release of gaseous NO and N2O. The potential biological relevance of this chemistry is discussed.
登录
查看更多内容
影响因子：
4.6
作者：
Chang, SC;Karambelkar, VV;Goldberg, DP
通讯作者：
Goldberg, DP
影响因子：
4.8
作者：
Kröncke, KD;Klotz, LO;Sies, H
通讯作者：
Sies, H
影响因子：
2.9
作者：
Mitchell, DA;Erwin, PA;Marletta, MA
通讯作者：
Marletta, MA
影响因子：
2.9
作者：
Ghosh, DK;Wu, CQ;Stuehr, DJ
通讯作者：
Stuehr, DJ
影响因子：
4.6
作者：
Andersen, Ryan J.;diTargiani, Robert C.;Godwin, Hilary A.
通讯作者：
Godwin, Hilary A.