Key laboratory for Molecular Enzymology and Engineering, the Ministry of Education, Collage of Life Science, Jilin University, Changchun 130012, PR China.
CAS Key Laboratory for Biomedical Effects of Nanomaterials & Nanosafety, National Center for Nanoscience and Technology of China, Beijing 100190, PR China.
Biosens Bioelectron. 2015 Feb 15;64:165-70. doi: 10.1016/j.bios.2014.08.078. Epub 2014 Sep 3.
The discovery and application of noble metal nanoclusters have received considerable attention. In this paper, we reported that apoferritin paired gold clusters (Au-Ft) could efficiently catalyze oxidation of 3.3',5.5'-tetramethylbenzidine (TMB) by H2O2 to produce a blue color reaction. Compared with natural enzyme, Au-Ft exhibited higher activity near acidic pH and could be used over a wide range of temperatures. Apoferritin nanocage enhanced the reaction activity of substrate TMB by H2O2. The reaction catalyzed by Au-Ft was found to follow a typical Michaelis-Menten kinetics. The kinetic parameters exhibited a lower K(m) value (0.097 mM) and a higher K(cat) value (5.8 × 10(4) s(-1)) for TMB than that of horse radish peroxidase (HRP). Base on these findings, Au-Ft, acting as a peroxidase mimetic, performed enzymatic spectrophotometric analysis of glucose. This system exhibited acceptable reproducibility and high selectivity in biosening, suggesting that it could have promising applications in the future.
贵金属纳米团簇的发现和应用受到了广泛关注。本文报道了脱铁铁蛋白偶联金纳米团簇（Au-Ft）可以高效地催化 H2O2 氧化 3,3',5,5'-四甲基联苯胺（TMB）产生蓝色显色反应。与天然酶相比，Au-Ft 在近酸性 pH 值下表现出更高的活性，并且可以在较宽的温度范围内使用。脱铁铁蛋白纳米笼增强了 H2O2 作用下底物 TMB 的反应活性。Au-Ft 催化的反应被发现遵循典型的米氏动力学。对于 TMB，动力学参数表现出较低的 K(m) 值（0.097 mM）和较高的 K(cat) 值（5.8×10(4) s(-1)），均优于辣根过氧化物酶（HRP）。基于这些发现，Au-Ft 作为过氧化物酶模拟物，对葡萄糖进行了酶分光光度分析。该系统在生物传感中表现出可接受的重现性和高选择性，表明它在未来可能有有前景的应用。
