Flavin–Protein Complexes: Aromatic Stacking Assisted by a Hydrogen Bond,Biochemistry

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Flavin–Protein Complexes: Aromatic Stacking Assisted by a Hydrogen Bond
Biochemistry ( IF 2.9 ) Pub Date : 2015-07-08 00:00:00 , DOI: 10.1021/acs.biochem.5b00501
Djemel Hamdane ₁ , Charles Bou-Nader ₁ , David Cornu ₂ , Gaston Hui-Bon-Hoa ₃ , Marc Fontecave ₁

Affiliation

Enzyme-catalyzed reactions often rely on a noncovalently bound cofactor whose reactivity is tuned by its immediate environment. Flavin cofactors, the most versatile catalyst encountered in biology, are often maintained within the protein throughout numbers of complex ionic and aromatic interactions. Here, we have investigated the role of π–π stacking and hydrogen bond interactions between a tyrosine and the isoalloxazine moiety of the flavin adenine dinucleotide (FAD) in an FAD-dependent RNA methyltransferase. Combining several static and time-resolved spectroscopies as well as biochemical approaches, we showed that aromatic stacking is assisted by a hydrogen bond between the phenol group and the amide of an adjacent active site loop. A mechanism of recognition and binding of the redox cofactor is proposed.

中文翻译：

黄素-蛋白质复合物：氢键辅助的芳香堆积

酶催化的反应通常依赖于非共价结合的辅因子，其反应性受其直接环境调节。黄素辅因子是生物学上最通用的催化剂，通常在整个复杂的离子和芳族相互作用中一直保持在蛋白质中。在这里，我们研究了FAD依赖的RNA甲基转移酶中酪氨酸和黄素腺嘌呤二核苷酸（FAD）的异阿洛嗪部分之间的π-π堆积和氢键相互作用的作用。结合几种静态的和时间分辨的光谱学以及生化方法，我们显示了芳香族堆积是由酚基团和相邻活性位点环的酰胺之间的氢键辅助的。提出了氧化还原辅因子的识别和结合机制。

更新日期：2015-07-08

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