Caseoperoxidase, mixed β-casein-SDS-hemin-imidazole complex: a nano artificial enzyme.
Caseoperoxidase, mixed β-casein-SDS-hemin-imidazole complex: a nano artificial enzyme.
复制标题
酪过氧化物酶，混合β-酪蛋白-SDS-血红素-咪唑复合物：一种纳米人工酶。
DOI：
10.1080/07391102.2014.1003196
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发表时间：
2015
影响因子：
4.4
通讯作者：
Moosavi-Mova
中科院分区：
文献类型：
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作者：
Moosavi-Movahedi,Zainab;Gharibi,Hussein;Hadi-Alijanvand,Hamid;Akbarzadeh,Mohammad;Esmaili,Mansoore;Atri,MalihehS;Sefidbakht,Yahya;Bohlooli,Mousa;Nazari,Khodadad;Javadian,Soheila;Hong,Jun;Saboury,AliA;Sheibani,Nader;Moosavi-Mova
利用纳米人工氨基酸载脂蛋白疏水口袋仿生设计了一种新型过氧化物酶样人工酶，称为“酪蛋白过氧化物酶”。这种含有血红素-咪唑-β-酪蛋白-SDS 的四组分纳米人工酶对天然辣根过氧化物酶表现出高活性生长和 kcat 性能，通过使用紫外可见分光光度法的稳态动力学证明。通过ANS荧光和圆二色光谱研究了酪过氧化物酶的疏水性和二级结构。骆驼β-酪蛋白(Cβ-酪蛋白)因其固有的灵活性和较高的疏水性而被选为血红素活性位点的合适的脱辅基蛋白。该选择通过同源建模方法得到证实。血红素与新获得的 Cβ-酪蛋白结构对接表明一种血红素主要与 Cβ-酪蛋白结合。 Cβ-酪蛋白中活性位点的主要静电位点的存在也通过怀曼结合电位和等温滴定量热法的实验方法得到证实。该生物催化剂中 Cβ-酪蛋白的存在降低了自杀失活，并为血红素活性位点提供了适当的保护作用。其他实验证实了酪过氧化物酶作为人工酶的结构和功能的保留。
A novel peroxidase-like artificial enzyme, named “caseoperoxidase”, was biomimetically designed using a nano artificial amino acid apo-protein hydrophobic pocket. This four-component nano artificial enzyme containing heme–imidazole–β-casein–SDS exhibited high activity growth andkcatperformance toward the native horseradish peroxidase demonstrated by the steady state kinetics using UV–vis spectrophotometry. The hydrophobicity and secondary structure of the caseoperoxidase were studied by ANS fluorescence and circular dichroism spectroscopy.Camel β-casein (Cβ-casein) was selected as an appropriate apo-protein for the heme active site because of its innate flexibility and exalted hydrophobicity. This selection was confirmed by homology modeling method. Heme docking into the newly obtained Cβ-casein structure indicated one heme was mainly incorporated with Cβ-casein. The presence of a main electrostatic site for the active site in the Cβ-casein was also confirmed by experimental methods through Wyman binding potential and isothermal titration calorimetry. The existence of Cβ-casein protein in this biocatalyst lowered the suicide inactivation and provided a suitable protective role for the heme active-site. Additional experiments confirmed the retention of caseoperoxidase structure and function as an artificial enzyme.