Chemical activation of cytochrome c proteins via crown ether complexation:: Cold-active synzymes for enantiomer-selective sulfoxide oxidation in methanol
Chemical activation of cytochrome c proteins via crown ether complexation:: Cold-active synzymes for enantiomer-selective sulfoxide oxidation in methanol
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DOI：
10.1021/ja037239a
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发表时间：
2003-09-24
影响因子：
15
通讯作者：
Tsukube, H
中科院分区：
文献类型：
--
作者：
Paul, D;Suzumura, A;Tsukube, H
与18-冠-6的超分子络合显着地将无催化活性的细胞色素（生物形式）转化为催化活性的合成酶（人工形式）。虽然细胞色素蛋白家族在自然界中不像酶那样起作用，但冠醚络合修饰了它们的血红素配位结构，并功能性地激活了它们，以促进外消旋亚砜在低温下的不对称氧化。马心、鸽胸和酵母细胞色素蛋白在甲醇中与18-冠-6形成超分子复合物，在−40 °C下有效氧化萘甲基亚砜、甲基甲苯基亚砜、异丙基苯基亚砜、苄基甲基亚砜和4-甲硫基苯乙酮的（S）-异构体。由于马心和鸽胸细胞色素比酵母细胞色素具有更高的对映体选择性和更高的活性，细胞色素与冠醚的适当组合提供了一类新的促进非生物不对称氧化的冷活性合酶。
Supramolecular complexation with 18-crown-6 significantly converted catalytically inactive cytochromec(biological form) to catalytically active synzyme (artificial form). Although a family of cytochromecproteins does not work as enzymes in nature, crown ether complexation modified their heme coordination structures and functionally activated them to promote the asymmetric oxidation of racemic sulfoxides at low temperature. Horse heart, pigeon breast, and yeast cytochromecproteins were demonstrated to form supramolecular complexes with 18-crown-6 in methanol, which effectively oxidized (S)-isomers of naphthyl methyl sulfoxide, methyl tolyl sulfoxide, isopropyl phenyl sulfoxide, benzyl methyl sulfoxide, and 4-methylsulfenyl acetophenone at −40 °C. Because horse heart and pigeon breast cytochromescexhibited more efficient and higher enantiomer-selective activities than yeast cytochromec, a proper combination of cytochromecand crown ether offers a new class of cold-active synzymes promoting nonbiological asymmetric oxidation.