Titelbild: A Cytochrome P450 TxtE Model System with Mechanistic and Theoretical Evidence for a Heme Peroxynitrite Active Species (Angew. Chem. 49/2024)
Pritam Mondal, Dhilanka Udukalage, Abubaker A. Mohamed, Henrik P. H. Wong, Sam P. de Visser, Gayan B. Wijeratne
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引用次数: 0
Abstract
Tryptophan nitration chemistry of an economically impactful heme enzyme, TxtE, has been modeled utilizing synthetic heme mimics by Sam P. de Visser, Gayan B. Wijeratne et al. in their Research Article (e202409430). Therein, spectroscopic and theoretical characterizations strongly suggest the occurrence of a heme peroxynitrite active species, closely paralleling mechanistic propositions put forward for TxtE enzyme. Precise mechanistic details and key structure–activity relationships present important findings to be implemented in next generation therapeutic and synthetic applications.
Sam P. de Visser、Gayan B. Wijeratne 等人在他们的研究文章 (e202409430) 中利用合成血红素模拟物对一种具有经济影响的血红素酶 TxtE 的色氨酸硝化化学进行了建模。Wijeratne 等人在其研究文章 (e202409430) 中利用合成血红素模拟物建立了一个模型。在这篇文章中，光谱和理论特征都有力地证明了血红素过亚硝酸盐活性物种的存在，这与 TxtE 酶提出的机理命题密切相关。精确的机理细节和关键的结构-活性关系提供了重要的发现，可用于下一代治疗和合成应用。
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