Dataset Information

A Cost-Effective Hemin-Based Artificial Enzyme Allows for Practical Applications.

ABSTRACT: Nanomaterials excel in mimicking the structure and function of natural enzymes while being far more interesting in terms of structural stability, functional versatility, recyclability, and large-scale preparation. Herein, the story assembles hemin, histidine analogs, and G-quadruplex DNA in a catalytically competent supramolecular assembly referred to as assembly-activated hemin enzyme (AA-heminzyme). The catalytic properties of AA-heminzyme are investigated both in silico (by molecular docking and quantum chemical calculations) and in vitro (notably through a systematic comparison with its natural counterpart horseradish peroxidase, HRP). It is found that this artificial system is not only as efficient as HRP to oxidize various substrates (with a turnover number k_cat of 115 s^-1) but also more practically convenient (displaying better thermal stability, recoverability, and editability) and more economically viable, with a catalytic cost amounting to <10% of that of HRP. The strategic interest of AA-heminzyme is further demonstrated for both industrial wastewater remediation and biomarker detection (notably glutathione, for which the cost is decreased by 98% as compared to commercial kits).

SUBMITTER: Qiu D

PROVIDER: S-EPMC11348135 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

A Cost-Effective Hemin-Based Artificial Enzyme Allows for Practical Applications.

Qiu Dehui D He Fangni F Liu Yuan Y Zhou Zhaoxi Z Yang Yuqin Y Long Zhongwen Z Chen Qianqian Q Chen Desheng D Wei Shijiong S Mao Xuanxiang X Zhang Xiaobo X Mergny Jean-Louis JL Monchaud David D Ju Huangxian H Zhou Jun J

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20240625 32

Nanomaterials excel in mimicking the structure and function of natural enzymes while being far more interesting in terms of structural stability, functional versatility, recyclability, and large-scale preparation. Herein, the story assembles hemin, histidine analogs, and G-quadruplex DNA in a catalytically competent supramolecular assembly referred to as assembly-activated hemin enzyme (AA-heminzyme). The catalytic properties of AA-heminzyme are investigated both in silico (by molecular docking ...[more]

PMID: 38924304

Similar Datasets

Project description:When fabricating Si-based devices, many process steps require the use of expensive, high-power consumption, environmentally unfriendly, operator-unsafe machines, and processes. Among the many involved process steps, the ones needed to fabricate the metallurgical junction make use of conventional doping methods, which do not always represent optimal solutions. The high costs of the processing equipment and the use of hazardous materials, not to count the structural damage produced, intrinsically limit future developments towards nm-scaled and low cost approaches. Recently a chemistry-based method has been proposed to form the junction on Si, the so-called molecular doping. In this approach, the samples to be doped are subjected to a silylation process, during which a layer of dopant-containing molecules is deposited in a liquid bath kept at boiling temperature. After the coating, the samples are annealed to decompose the molecule and release the dopants inside the target. The peculiarity of using a liquid source allows for avoiding the structural damage. The entire doping procedure is simple and cost-effective, and it is based on the use of ester molecules, which are less harmful than the standard materials. In this work, we present experimental results on this chemistry-based technique, demonstrating its efficiency in creating the junction and demonstrate its feasibility in the fabrication of solar cells prototypes. Moreover, with respect to the literature, we show for the first time the effects of the protective layer presence over the dopant source molecules in the final solar cells electrical properties. As a proof of concept, we have numerically investigated the Si-based solar cell using the SCPAS-1D simulator. The finding claims that, the proposed samples have a good match in terms of the performance of the devices compared to the conventional Si-solar cells. Henceforth, the proposed work can provide a guideline to achieve less expensive, more environmentally friendly techniques for molecular doping in Si without affecting its performance in the metallurgical junction.

Dataset Information

A Cost-Effective Hemin-Based Artificial Enzyme Allows for Practical Applications.

Publications

A Cost-Effective Hemin-Based Artificial Enzyme Allows for Practical Applications.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets