Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo náměstí 2, 166 10, Praha 6, Czech Republic.
Chem Commun (Camb). 2022 Mar 22;58(24):3913-3916. doi: 10.1039/d2cc00750a.
The factors that control the diverse reactivity of the μ-η:η-peroxo dicopper(II) oxy-intermediates in the coupled binuclear copper proteins remain elusive. Here, spectroscopic and computational methods reveal H-bonding interactions between active-site waters and the μ-η:η-peroxide of oxy-tyrosinase, and define their effects on the Cu(II)O electronic structure and O activation.
控制偶联双核铜蛋白中 μ-η:η-过氧二铜(II)氧中间物的不同反应性的因素仍然难以捉摸。在这里,光谱和计算方法揭示了酪氨酸氧化酶活性位点水中氢键相互作用与 μ-η:η-过氧化物,定义了它们对 Cu(II)O 电子结构和 O 激活的影响。