天青
化学
S-亚硝基化
亚硝化
半胱氨酸
组合化学
金属蛋白
合理设计
铜蛋白
铜
酶
氧化还原
生物物理学
生物化学
纳米技术
一氧化氮
无机化学
有机化学
生物
材料科学
作者
Shiliang Tian,Jing Liu,Ryan E. Cowley,Parisa Hosseinzadeh,Nicholas Marshall,Yang Yu,Howard Robinson,Mark J. Nilges,Ninian J. Blackburn,Edward I. Solomon,Yi Lu
出处
期刊:Nature Chemistry
[Springer Nature]
日期:2016-04-25
卷期号:8 (7): 670-677
被引量:41
摘要
S-Nitrosothiols are known as reagents for NO storage and transportation and as regulators in many physiological processes. Although the S-nitrosylation catalysed by haem proteins is well known, no direct evidence of S-nitrosylation in copper proteins has been reported. Here, we report reversible insertion of NO into a copper-thiolate bond in an engineered copper centre in Pseudomonas aeruginosa azurin by rational design of the primary coordination sphere and tuning its reduction potential by deleting a hydrogen bond in the secondary coordination sphere. The results not only provide the first direct evidence of S-nitrosylation of Cu(II)-bound cysteine in metalloproteins, but also shed light on the reaction mechanism and structural features responsible for stabilizing the elusive Cu(I)-S(Cys)NO species. The fast, efficient and reversible S-nitrosylation reaction is used to demonstrate its ability to prevent NO inhibition of cytochrome bo3 oxidase activity by competing for NO binding with the native enzyme under physiologically relevant conditions.
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