通过加速从 Fe3+ 到 Fe2+ 的转化提高 Fe0.8Ni0.2S2 类过氧化物酶的活性,The Journal of Physical Chemistry C

当前位置： X-MOL 学术 › J. Phys. Chem. C › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

通过加速从 Fe3+ 到 Fe2+ 的转化提高 Fe0.8Ni0.2S2 类过氧化物酶的活性
The Journal of Physical Chemistry C ( IF 3.3 ) Pub Date : 2022-02-23 , DOI: 10.1021/acs.jpcc.1c10325
Chengyu Zhang ₁ , Zhaodong Nan ₁

Affiliation

在过去的几十年里，纳米酶被认为是天然酶的强有力替代品。然而，由于纳米酶的活性低，总是需要高浓度的底物，这导致实际应用中成本的增加和环境污染的增加。因此，改善纳米酶活性对于减少对高浓度底物的需求仍然是紧迫且至关重要的。首先通过水热法合成了一系列具有纳米酶活性的二元金属硫化物（Fe _x Ni _{1– x} S _{2 ）。}在这些样品中，纳米片状的Fe _0.8 Ni _0.2 S ₂表现出最高的活性。与 FeS 相比_如图2所示， Fe _0.8 Ni _0.2 S ₂的催化常数( K _cat )和催化效率( K _cat / K _m )分别提高了约1.9倍和3.6倍。Fe _0.8 Ni _0.2 S ₂的米氏常数（K _m ）比FeS ₂小4.7倍，比天然酶辣根过氧化物酶（HRP）小193倍，表明对H的亲和力更强₂ O ₂。机理研究表明，Fe ²⁺和 FeFe _0.8 Ni _0.2 S _2中的³⁺是活性位点。Ni ²⁺和Fe ³⁺的协同作用加速了Fe ³⁺向Fe ²⁺的转化，从而提高了纳米酶的活性。此外，Fe _0.8 Ni _0.2 S ₂可用作纳米酶，在室温（25℃）下1分钟内检测H ₂ O _{2和抗坏血酸（AA）。}这项工作扩展了二元金属硫化物作为人工酶的开发。

"点击查看英文标题和摘要"

Improvement of Fe0.8Ni0.2S2 Peroxidase-like Activity through the Accelerated Conversion from Fe3+ to Fe2+

Nanoenzymes have been regarded as strong substitutes to natural enzymes in the last decades. However, high concentrations of substrates are always needed because of the low activity of nanozymes, which causes an increase of the cost and an increase in environmental pollution in practical applications. Thus, improved nanozymic activity is still urgent and vital to reduce the need for high concentrations of substrates. A series of binary metal sulfides (Fe_xNi_1–xS₂), which exhibited intrinsic nanozymic activity, was first synthesized by a hydrothermal method. Among these samples, the nanosheet-shaped Fe_0.8Ni_0.2S₂ showed the highest activity. Compared with those of FeS₂, the catalytic constant (K_cat) and catalytic efficiency (K_cat/K_m) of Fe_0.8Ni_0.2S₂ increased about 1.9 and 3.6 times, respectively. The Michaelis–Menten constant (K_m) of Fe_0.8Ni_0.2S₂ is about 4.7-fold smaller than that of FeS₂, and 193-fold smaller than that of natural enzyme horseradish peroxidase (HRP), indicating a stronger affinity to H₂O₂. The investigation on the mechanism indicated that Fe²⁺ and Fe³⁺ in Fe_0.8Ni_0.2S₂ are the active sites. The synergistic effect between Ni²⁺ and Fe³⁺ accelerated the conversion from Fe³⁺ to Fe²⁺, which improved the nanozymic activity. In addition, Fe_0.8Ni_0.2S₂ can be used as a nanozyme to detect H₂O₂ and ascorbic acid (AA) within 1 min at room temperature (25 °C). This work extends the development of binary metal sulfides as artificial enzymes.

更新日期：2022-02-23

点击分享查看原文

点击收藏

阅读更多本刊新发论文本刊介绍/投稿指南