一锅法合成硝基环丙烷:α-淀粉酶催化Michael加成引发环闭合序列反应

Xue-Dong Zhang, Jian Song, Na Gao, Zhi Guan, Yan-Hong He
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引用次数: 4

摘要

本文介绍了溴环烷与α,β-不饱和烯酮通过迈克尔加成引发的环闭合顺序反应一锅合成硝基环丙烷的方法。以猪胰腺α-淀粉酶为催化剂,得到了较好的收率(55 ~ 93%)和一定的对映选择性。该策略利用酶的非自然能力,为绿色有机合成提供了一种方便的生物催化方法。
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One-pot synthesis of nitrocyclopropane: α-Amylase-catalyzed Michael addition initiated ring-closure sequence reactions

This article presents a one-pot synthesis of nitrocyclopropanes via Michael addition initiated ring-closure sequence reactions of bromonitroalkane to α,β-unsaturated enones. Moderate to favorable yields (55–93%) and certain enantioselectivities were obtained with α-amylase from hog pancreas as the catalyst. This strategy utilizes the unnatural ability of enzymes to provide a convenient and biocatalytic method for green organic synthesis.

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来源期刊
Journal of Molecular Catalysis B-enzymatic
Journal of Molecular Catalysis B-enzymatic 生物-生化与分子生物学
CiteScore
2.58
自引率
0.00%
发文量
0
审稿时长
3.4 months
期刊介绍: Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation. Papers should report novel and significant advances in one or more of the following topics; Applied and fundamental studies of enzymes used for biocatalysis; Industrial applications of enzymatic processes, e.g. in fine chemical synthesis; Chemo-, regio- and enantioselective transformations; Screening for biocatalysts; Integration of biocatalytic and chemical steps in organic syntheses; Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies; Enzyme immobilization and stabilization, particularly in non-conventional media; Bioprocess engineering aspects, e.g. membrane bioreactors; Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification; Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity; Biomimetic studies related to enzymatic transformations.
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