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Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins
Journal of the American Chemical Society ( IF 15.0 ) Pub Date : 2017-11-15 00:00:00 , DOI: 10.1021/jacs.7b10452
Samuel I. Mann 1 , Tillmann Heinisch 2 , Thomas R. Ward 2 , A. S. Borovik 1
Affiliation  

Copper–hydroperoxido species (CuII–OOH) have been proposed to be key intermediates in biological and synthetic oxidations. Using biotin–streptavidin (Sav) technology, artificial copper proteins have been developed to stabilize a CuII–OOH complex in solution and in crystallo. Stability is achieved because the Sav host provides a local environment around the Cu–OOH that includes a network of hydrogen bonds to the hydroperoxido ligand. Systematic deletions of individual hydrogen bonds to the Cu–OOH complex were accomplished using different Sav variants and demonstrated that stability is achieved with a single hydrogen bond to the proximal O-atom of the hydroperoxido ligand: changing this interaction to only include the distal O-atom produced a reactive variant that oxidized an external substrate.

中文翻译:

人工铜蛋白中氢键调节的过氧化物活化

铜-氢过氧化物(Cu II -OOH)被提议为生物和合成氧化的关键中间体。利用生物素-链霉亲和素(Sav)技术,已开发出人造铜蛋白来稳定溶液中和晶体中的Cu II -OOH复合物。之所以能够实现稳定性,是因为Sav宿主在Cu-OOH周围提供了一个局部环境,其中包括与氢过氧化物配体形成氢键的网络。使用不同的Sav变体对Cu-OOH络合物的单个氢键进行系统性删除,并证明了通过与氢过氧化物配体的近端O原子的单个氢键即可实现稳定性:将这种相互作用改变为仅包括远端O-原子产生的反应性变体氧化了外部底物。
更新日期:2017-11-16
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