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Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage
Ascorbate peroxidase (APX) as a crucial antioxidant enzyme has drawn attentions for its utilization in preventing cells from oxidative stress responses by efficiently scavenging H(2)O(2) in plants. For eliminating the specific inactivation of natural APXs and regulating the catalytic activity, singl...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8844488/ https://www.ncbi.nlm.nih.gov/pubmed/34951150 http://dx.doi.org/10.1002/advs.202103977 |
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author | Chen, Yuan Zou, Hang Yan, Bo Wu, Xiaoju Cao, Weiwei Qian, Yihang Zheng, Lei Yang, Guowei |
author_facet | Chen, Yuan Zou, Hang Yan, Bo Wu, Xiaoju Cao, Weiwei Qian, Yihang Zheng, Lei Yang, Guowei |
author_sort | Chen, Yuan |
collection | PubMed |
description | Ascorbate peroxidase (APX) as a crucial antioxidant enzyme has drawn attentions for its utilization in preventing cells from oxidative stress responses by efficiently scavenging H(2)O(2) in plants. For eliminating the specific inactivation of natural APXs and regulating the catalytic activity, single‐atom nanozymes are considered as promising classes of alternatives with similar active sites and maximal atomic utilization efficiency to natural APXs. Herein, graphitic carbon nitride (g‐C(3)N(4)) anchored with isolated single copper atoms (Cu SAs/CN) is designed as an efficient nanozyme with intrinsic APX mimetic behavior. The engineered Cu SAs/CN exhibits comparable specific activity and kinetics to the natural APXs. Based on the density functional theory (DFT), Cu‐N(4) moieties in the active center of Cu SAs/CN are determined to exert such favorable APX catalytic performance, in which the electron transfer between Cu and coordinated N atoms facilitates the activation and cleavage of the adsorbed H(2)O(2) molecules and results in fast kinetics. The constructed Cu SAs/CN nanozyme with superior APX‐like performance and high biocompatibility can be applied for effectively protecting the H(2)O(2)‐treated cells against oxidative injury in vitro. These findings report the single‐atom nanozymes as a successful paradigm for guiding nanozymes to implement APX mimetic performance for reactive oxygen species‐related biotherapeutic. |
format | Online Article Text |
id | pubmed-8844488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88444882022-02-24 Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage Chen, Yuan Zou, Hang Yan, Bo Wu, Xiaoju Cao, Weiwei Qian, Yihang Zheng, Lei Yang, Guowei Adv Sci (Weinh) Research Articles Ascorbate peroxidase (APX) as a crucial antioxidant enzyme has drawn attentions for its utilization in preventing cells from oxidative stress responses by efficiently scavenging H(2)O(2) in plants. For eliminating the specific inactivation of natural APXs and regulating the catalytic activity, single‐atom nanozymes are considered as promising classes of alternatives with similar active sites and maximal atomic utilization efficiency to natural APXs. Herein, graphitic carbon nitride (g‐C(3)N(4)) anchored with isolated single copper atoms (Cu SAs/CN) is designed as an efficient nanozyme with intrinsic APX mimetic behavior. The engineered Cu SAs/CN exhibits comparable specific activity and kinetics to the natural APXs. Based on the density functional theory (DFT), Cu‐N(4) moieties in the active center of Cu SAs/CN are determined to exert such favorable APX catalytic performance, in which the electron transfer between Cu and coordinated N atoms facilitates the activation and cleavage of the adsorbed H(2)O(2) molecules and results in fast kinetics. The constructed Cu SAs/CN nanozyme with superior APX‐like performance and high biocompatibility can be applied for effectively protecting the H(2)O(2)‐treated cells against oxidative injury in vitro. These findings report the single‐atom nanozymes as a successful paradigm for guiding nanozymes to implement APX mimetic performance for reactive oxygen species‐related biotherapeutic. John Wiley and Sons Inc. 2021-12-23 /pmc/articles/PMC8844488/ /pubmed/34951150 http://dx.doi.org/10.1002/advs.202103977 Text en © 2021 The Authors. Advanced Science published by Wiley‐VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Chen, Yuan Zou, Hang Yan, Bo Wu, Xiaoju Cao, Weiwei Qian, Yihang Zheng, Lei Yang, Guowei Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title | Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title_full | Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title_fullStr | Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title_full_unstemmed | Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title_short | Atomically Dispersed Cu Nanozyme with Intensive Ascorbate Peroxidase Mimic Activity Capable of Alleviating ROS‐Mediated Oxidation Damage |
title_sort | atomically dispersed cu nanozyme with intensive ascorbate peroxidase mimic activity capable of alleviating ros‐mediated oxidation damage |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8844488/ https://www.ncbi.nlm.nih.gov/pubmed/34951150 http://dx.doi.org/10.1002/advs.202103977 |
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