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Exploiting and Engineering Neuroglobin for Catalyzing Carbene N-H Insertions and the Formation of Quinoxalinones

文献类型： 外文期刊

作者： Sun, Li-Juan 1 ; Wang, Huamin 2 ; Xu, Jia-Kun 3 ; Gao, Shu-Qin 1 ; Wen, Ge-Bo 1 ; Lin, Ying-Wu 1 ;

作者机构： 1.Univ South China, Hengyang Med Sch, Hengyang 421001, Peoples R China

2.Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Polar Fishery, Qingdao 266071, Peoples R China

期刊名称：INORGANIC CHEMISTRY （ 2022影响因子：4.6； 五年影响因子：4.4 ）

ISSN： 0020-1669

年卷期： 2023 年 62 卷 40 期

页码：

收录情况： SCI

摘要： It is desired to design and construct more efficient enzymes with better performance to catalyze carbene N-H insertions for the synthesis of bioactive molecules. To this end, we exploited and designed a series of human neuroglobin (Ngb) mutants. As shown in this study, a double mutant, A15C/H64G Ngb, with an additional disulfide bond and a modified heme active site, exhibited yields up to >99% and total turnover numbers up to 33000 in catalyzing the carbene N-H insertions for aromatic amine derivatives, including those with a large size such as 1-aminopyrene. Moreover, for o-phenylenediamine derivatives, they underwent two cycles of N-H insertions, followed by cyclization to form quinoxalinones, as confirmed by the X-ray crystal structures. This study suggests that Ngb can be designed into a functional carbene transferase for efficiently catalyzing carbene N-H insertion reactions with a range of substrates. It also represents the first example of the formation of quinoxalinones catalyzed by an engineered heme enzyme.

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