Copper-Oxygen Dynamics in the Tyrosinase Mechanism.,Angewandte Chemie International Edition

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Copper-Oxygen Dynamics in the Tyrosinase Mechanism.
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2020-04-30 , DOI: 10.1002/anie.202004733
Nobutaka Fujieda ₁ , Kyohei Umakoshi ₂ , Yuta Ochi ₁ , Yosuke Nishikawa ₃ , Sachiko Yanagisawa ₄ , Minoru Kubo ₄ , Genji Kurisu ₃ , Shinobu Itoh ₂

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The dinuclear copper enzyme, tyrosinase, activates O₂ to form a (μ‐η²:η²‐p eroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X‐ray crystal structures of the active tyrosinases with substrate l ‐tyrosine. At their catalytic sites, CuA moved toward l ‐tyrosine (CuA1 → CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 → CuB2). The crystal structures and spectroscopic analyses of the dioxygen‐bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O−O bond. Thus, the copper migration induced by the substrate‐binding is accompanied by rearrangement of the bound peroxide species so as to provide one of the peroxide oxygen atoms with access to the phenol substrate's ϵ carbon atom.

中文翻译：

酪氨酸酶机制中的铜氧动力学。

双核铜酶，酪氨酸酶，激活Ò ₂，以形成（μ-η ²：η ² -p eroxido）亚铜（II）种，其中羟基化酚以儿茶酚。然而，在酪氨酸酶催化位点酚酶反应的确切机理仍在争论中。我们在此报告了具有底物l酪氨酸的活性酪氨酸酶的近原子分辨率X射线晶体结构。在他们的催化位点，CUA移向升-酪氨酸（CuA1→CuA2），其苯酚氧直接与CuA2配位，涉及CuB（CuB1→CuB2）的运动。双氧结合酪氨酸酶的晶体结构和光谱分析表明，过氧化物配体旋转，自发地减弱了其O-O键。因此，由底物结合引起的铜迁移伴随着结合的过氧化物种类的重排，从而使过氧化物中的一个氧原子能够接近酚底物的ϵ 碳原子。

更新日期：2020-04-30

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