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Enzymatic assembly of carbon-carbon bonds via iron-catalysed sp~3 C-H functionalization

机译：铁催化的sp〜3 C-H官能化酶催化碳-碳键的组装

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摘要

Although abundant in organic molecules, carbon-hydrogen (C-H) bonds are typically considered unreactive and unavailable for chemical manipulation. Recent advances in C-H functionalization technology have begun to transform this logic, while emphasizing the importance of and challenges associated with selective alkylation at a sp(3) carbon(1,2). Here we describe iron-based catalysts for the enantio-, regio- and chemoselective intermolecular alkylation of sp(3) C-H bonds through carbene C-H insertion. The catalysts, derived from a cytochrome P450 enzyme in which the native cysteine axial ligand has been substituted for serine (cytochrome P411), are fully genetically encoded and produced in bacteria, where they can be tuned by directed evolution for activity and selectivity. That these proteins activate iron, the most abundant transition metal, to perform this chemistry provides a desirable alternative to noble-metal catalysts, which have dominated the field of C-H functionalization(1,2). The laboratory-evolved enzymes functionalize diverse substrates containing benzylic, allylic or alpha-amino C-H bonds with high turnover and excellent selectivity. Furthermore, they have enabled the development of concise routes to several natural products. The use of the native iron-haem cofactor of these enzymes to mediate sp( )(3)C-H alkylation suggests that diverse haem proteins could serve as potential catalysts for this abiological transformation, and will facilitate the development of new enzymatic C-H functionalization reactions for applications in chemistry and synthetic biology.
机译：尽管有机分子中含量很高，但通常认为碳氢键（C-H）不具有反应性，无法进行化学操作。 C-H功能化技术的最新进展已开始转变这种逻辑，同时强调了在sp（3）碳（1,2）上进行选择性烷基化的重要性和挑战。在这里我们描述了通过卡宾C-H插入的sp（3）C-H键的对映，区域和化学选择性分子间烷基化的铁基催化剂。该催化剂衍生自细胞色素P450酶，其中天然半胱氨酸轴向配体已取代丝氨酸（细胞色素P411），并在细菌中进行了完全基因编码和生产，可在其中进行定向进化以调节其活性和选择性。这些蛋白质激活了铁（最丰富的过渡金属）以执行此化学反应，为贵金属催化剂提供了理想的替代方法，后者主导了C-H官能化领域（1,2）。实验室开发的酶以高周转率和出色的选择性功能化了含有苄基，烯丙基或α-氨基C-H键的多种底物。此外，它们还使开发一些天然产品的简洁路线成为可能。这些酶的天然铁血红素辅酶介导sp（）（3）CH烷基化的使用表明，多种血红素蛋白可以作为这种生物转化的潜在催化剂，并将促进新的酶促CH官能化反应的开发在化学和合成生物学领域。

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  • 来源
    《Nature》 |2019年第7737期|67-72|共6页
  • 作者

    Zhang Ruijie K.; Chen Kai; Huang Xiongyi; Wohlschlager Lena; Renata Hans; Arnold Frances H.;

  • 作者单位

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA;

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA;

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA;

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA|Univ Nat Resources & Life Sci, Inst Food Technol, Vienna, Austria;

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA|Scripps Res Inst, Dept Chem, Jupiter, FL USA;

    CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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