Calcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores
Calcium‐Ion Binding Mediates the Reversible Interconversion of Cis and Trans Peroxido Dicopper Cores
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钙离子结合介导顺式和反式过氧化物二铜核的可逆相互转化
DOI：
10.1002/anie.202105421
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Robinson, Jerome R.
中科院分区：
文献类型：
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作者：
Vargo, Natasha P.;Harland, Jill B.;Musselman, Bradley W.;Lehnert, Nicolai;Ertem, Mehmed Z.;Robinson, Jerome R.
III 型铜蛋白（血蓝蛋白、酪氨酸酶、儿茶酚氧化酶）中的耦合双核铜氧核心 (Cu2O2) 对于许多生物体中的 O2 运输和底物氧化至关重要。μ-1,2-顺过氧化二铜核心 (CP) 已被认为是这些蛋白质中 O2 结合早期阶段的关键结构；它们与其他 Cu2O2 核心的可逆异构化与酶功能直接相关。尽管此类物质与 III 型铜蛋白相关，并且人们对生物和合成系统中双金属 CP 核的性质和反应性更感兴趣，但 CPCu2O2 物质的性质和反应性在很大程度上仍未得到探索。在此，我们报道了μ-1,2-反式过氧化物（TP）和CP二铜核的可逆相互转化。 CaII 通过 Cu2O2 核心的可逆结合介导这一过程，突出了金属离子结合事件稳定新型反应片段并控制仿生系统中 O2 激活的独特能力。
Coupled dinuclear copper oxygen cores (Cu2O2) featured in type III copper proteins (hemocyanin, tyrosinase, catechol oxidase) are vital for O2transport and substrate oxidation in many organisms.μ‐1,2‐cisperoxido dicopper cores (CP) have been proposed as key structures in the early stages of O2binding in these proteins; their reversible isomerization to other Cu2O2cores are directly relevant to enzyme function. Despite the relevance of such species to type III copper proteins and the broader interest in the properties and reactivity of bimetallicCPcores in biological and synthetic systems, the properties and reactivity ofCPCu2O2species remain largely unexplored. Herein, we report the reversible interconversion ofμ‐1,2‐transperoxido (TP) andCPdicopper cores. CaIImediates this process by reversible binding at the Cu2O2core, highlighting the unique capability for metal‐ion binding events to stabilize novel reactive fragments and control O2activation in biomimetic systems.