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Schiff base complex conjugates of bovine serum albumin as artificial metalloenzymes for eco-friendly enantioselective sulfoxidation

机译:牛血清白蛋白席夫碱复合物作为人工金属酶,对环境友好的对映选择性硫氧化

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Artificial metalloenzymes (BSA- ML ) have been prepared by non-covalent insertion of transition metal Schiff-base complexes, ML (L = 2-hydroxynaphthalen-1-naphthaldehyde and 3,4-diaminobenzenesulfonic acid; M = Co, Mn, V, Fe, Cr), into bovine serum albumin (BSA) as the host protein and were characterized by UV-visible spectroscopy, ESI-TOF mass spectrometry and molecular docking studies. The catalytic activities of the BSA- ML in the selective oxidation of various prochiral sulfides in aqueous media, using H _(2) O _(2) as oxidant, have been evaluated. During the optimization process, pH and the concentrations of catalyst and oxidant were found to have a remarkable influence on both yield and enantioselectivity. In certain cases, BSA- ML gave satisfactory results in the oxidation of organic sulfides to sulfoxides (up to 100% conversion, 100% chemoselectivity, 96% ee and 500 h ~(?1) turnover frequency).
机译:人造金属酶(BSA- ML)是通过非共价插入过渡金属席夫碱配合物ML(L = 2-羟基萘-1-萘醛和3,4-二氨基苯磺酸; M = Co,Mn,V, Fe,Cr)转化为牛血清白蛋白(BSA)作为宿主蛋白,并通过紫外可见光谱,ESI-TOF质谱和分子对接研究进行了表征。使用H _(2)O _(2)作为氧化剂,评估了BSA-ML在水性介质中各种前手性硫化物的选择性氧化中的催化活性。在优化过程中,发现pH值以及催化剂和氧化剂的浓度对产率和对映选择性均具有显着影响。在某些情况下,BSA-ML在有机硫化物氧化为亚砜方面给出了令人满意的结果(高达100%的转化率,100%的化学选择性,96%ee和500 h〜(?1)转换频率)。

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