Functional and protective hole hopping in metalloenzymes,Chemical Science

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Functional and protective hole hopping in metalloenzymes
Chemical Science ( IF 7.6 ) Pub Date : 2021-09-27 , DOI: 10.1039/d1sc04286f
Harry B Gray ₁ , Jay R Winkler ₁

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Electrons can tunnel through proteins in microseconds with a modest release of free energy over distances in the 15 to 20 Å range. To span greater distances, or to move faster, multiple charge transfers (hops) are required. When one of the reactants is a strong oxidant, it is convenient to consider the movement of a positively charged “hole” in a direction opposite to that of the electron. Hole hopping along chains of tryptophan (Trp) and tyrosine (Tyr) residues is a critical function in several metalloenzymes that generate high-potential intermediates by reactions with O₂ or H₂O₂, or by activation with visible light. Examination of the protein structural database revealed that Tyr/Trp chains are common protein structural elements, particularly among enzymes that react with O₂ and H₂O₂. In many cases these chains may serve a protective role in metalloenzymes by deactivating high-potential reactive intermediates formed in uncoupled catalytic turnover.

中文翻译：

金属酶中的功能性和保护性空穴跳跃

电子可以在微秒内穿过蛋白质，并在 15 至 20 Å 范围内的距离内适度释放自由能。为了跨越更远的距离，或者移动得更快，需要多次电荷转移（跳跃）。当其中一种反应物是强氧化剂时，可以方便地考虑带正电的“空穴”沿与电子相反的方向移动。沿着色氨酸 (Trp) 和酪氨酸 (Tyr) 残基链的空穴跳跃是几种金属酶的关键功能，这些金属酶通过与 O ₂或 H ₂ O ₂反应或通过可见光激活产生高电位中间体。对蛋白质结构数据库的检查表明，Tyr/Trp 链是常见的蛋白质结构元件，特别是在与 O ₂和 H ₂ O ₂反应的酶中。在许多情况下，这些链可以通过使非偶联催化转换中形成的高电位反应中间体失活，在金属酶中发挥保护作用。

更新日期：2021-09-28

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