CAJ | 학술논문

近年来,催化氧化去除有机污染物受到越来越多的重视,但是氧气或过氧化氢绿色催化剂的使用因 O-O键活化的效率低下而受到限制。本文综述了不同种类氧化酶和加氧酶包括以多铜原子为中心(MCOs,如漆酶)和以卟啉/非卟啉铁为中心(HCOs,如细胞色素P450酶等)的氧化酶和加氧酶的 O-O 键活化机理。前者活性中心以4个铜原子组成,与其结合的氧气分子通过4电子过程实现 O-O 键断裂；后者主要以单个铁原子为活性中心,与铁配位的基团及铁的配合状态决定与其结合的氧气或过氧化氢分子中 O-O 键断裂机理。同时本文也对仿生催化材料在 O-O 键活化方面的工作进行了综述,其中主要包括对酶催化活性中心的模拟和支撑材料的选择。本综述旨在为 O-O 键活化的仿生催化剂设计和环境应用提供参考。
근년래,최화양화거제유궤오염물수도월래월다적중시,단시양기혹과양화경록색최화제적사용인 O-O건활화적효솔저하이수도한제。본문종술료불동충류양화매화가양매포괄이다동원자위중심(MCOs,여칠매)화이계람/비계람철위중심(HCOs,여세포색소P450매등)적양화매화가양매적 O-O 건활화궤리。전자활성중심이4개동원자조성,여기결합적양기분자통과4전자과정실현 O-O 건단렬；후자주요이단개철원자위활성중심,여철배위적기단급철적배합상태결정여기결합적양기혹과양화경분자중 O-O 건단렬궤리。동시본문야대방생최화재료재 O-O 건활화방면적공작진행료종술,기중주요포괄대매최화활성중심적모의화지탱재료적선택。본종술지재위 O-O 건활화적방생최화제설계화배경응용제공삼고。
Recently,increasing attention has been paid to the catalytic oxidation of many organic contaminants. However,the use of oxygen or hydrogen peroxide as the oxidant has low efficiency because of the difficulty of O-O bond activation.Major O-O bond activation mechanisms by oxydases and oxygenases were reviewed in order to gain insights to increase the efficiency of Fe and Cu based biocatalyst for molecular oxygen and hydrogen peroxide utilization in environmental remediation.Multicoppor oxidases(MCOs),e.g.laccase(Lc)use a cluster of three copper atoms and one distant copper as the active center.MCOs bind to oxygen atom and break O-O bond in the three-copper cluster through a four electron transfer process.Heme containing oxidases and oxygenases(HCOs)employ protonporphyrin IX coordinated iron(usually in six-coordinated state with one axils ligand)as the active center.The axils ligand facilitates the process of oxygen binding to Fe active site and O-O bond cleavage,while the mechanism varies in peroxidases and oxygenases.Non-heme oxidases and oxygenases(NHOs)also use iron as the active center, but iron is usually coordinated to amino acid residues instead of protonporphyrin IX ligand.Some progress on synthesis of biomimetic catalyst was also reviewed.Not only the active site but also the supporting media are demon-strated to affect the catalytic activity and reusability of the artificial enzymes.This review would provide useful infor-mation for enzyme application and design of biomimetic catalyst.