锌单原子纳米酶作为二氧化碳捕获和转化的碳酸酐酶模拟物。

IF 5.7 Q2 CHEMISTRY, PHYSICAL
ACS Materials Au Pub Date : 2025-01-31 eCollection Date: 2025-03-12 DOI:10.1021/acsmaterialsau.4c00156
Eslam M Hamed, Fun Man Fung, Sam F Y Li
{"title":"锌单原子纳米酶作为二氧化碳捕获和转化的碳酸酐酶模拟物。","authors":"Eslam M Hamed, Fun Man Fung, Sam F Y Li","doi":"10.1021/acsmaterialsau.4c00156","DOIUrl":null,"url":null,"abstract":"<p><p>Single-atom nanozymes (SANs) are a class of nanozymes with metal centers that mimic the structure of metalloenzymes. Herein, we report the synthesis of Zn-N-C SAN, which mimics the action of the natural carbonic anhydrase enzyme. The two-step annealing technique led to a metal content of more than 18 wt %. Since the metal centers act as active sites, this high metal loading resulted in superior catalytic activity. Zn-SAN showed a CO<sub>2</sub> uptake of 2.3 mmol/g and a final conversion of CO<sub>2</sub> to bicarbonate of more than 91%. CO<sub>2</sub> was converted via a biomimetic process by allowing its adsorption by the catalyst, followed by the addition of the catalyst to HEPES buffer (pH = 8) to start the CO<sub>2</sub> conversion into HCO<sub>3</sub> <sup>-</sup>. Afterward, CaCl<sub>2</sub> was added to form a white CaCO<sub>3</sub> precipitate, which was then filtered, dried, and weighed. Active carbon and MCM-41 were used as controls under the same reaction conditions. According to the findings, the CO<sub>2</sub> sequestration capacity was 42 mg of CaCO<sub>3</sub>/mg of Zn-SAN. Some amino acids (AAs) with binding affinity for Zn were able to suppress the enzymatic activity of Zn-SAN by blocking the active metal centers. This strategy was used for the detection of His, Cys, Glu, and Asp with detection limits of 0.011, 0.031, 0.029, and 0.062 μM, respectively, and hence was utilized for quantifying these AAs in commercial dietary supplements.</p>","PeriodicalId":29798,"journal":{"name":"ACS Materials Au","volume":"5 2","pages":"377-384"},"PeriodicalIF":5.7000,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11907284/pdf/","citationCount":"0","resultStr":"{\"title\":\"Zinc Single-Atom Nanozyme As Carbonic Anhydrase Mimic for CO<sub>2</sub> Capture and Conversion.\",\"authors\":\"Eslam M Hamed, Fun Man Fung, Sam F Y Li\",\"doi\":\"10.1021/acsmaterialsau.4c00156\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Single-atom nanozymes (SANs) are a class of nanozymes with metal centers that mimic the structure of metalloenzymes. Herein, we report the synthesis of Zn-N-C SAN, which mimics the action of the natural carbonic anhydrase enzyme. The two-step annealing technique led to a metal content of more than 18 wt %. Since the metal centers act as active sites, this high metal loading resulted in superior catalytic activity. Zn-SAN showed a CO<sub>2</sub> uptake of 2.3 mmol/g and a final conversion of CO<sub>2</sub> to bicarbonate of more than 91%. CO<sub>2</sub> was converted via a biomimetic process by allowing its adsorption by the catalyst, followed by the addition of the catalyst to HEPES buffer (pH = 8) to start the CO<sub>2</sub> conversion into HCO<sub>3</sub> <sup>-</sup>. Afterward, CaCl<sub>2</sub> was added to form a white CaCO<sub>3</sub> precipitate, which was then filtered, dried, and weighed. Active carbon and MCM-41 were used as controls under the same reaction conditions. According to the findings, the CO<sub>2</sub> sequestration capacity was 42 mg of CaCO<sub>3</sub>/mg of Zn-SAN. Some amino acids (AAs) with binding affinity for Zn were able to suppress the enzymatic activity of Zn-SAN by blocking the active metal centers. This strategy was used for the detection of His, Cys, Glu, and Asp with detection limits of 0.011, 0.031, 0.029, and 0.062 μM, respectively, and hence was utilized for quantifying these AAs in commercial dietary supplements.</p>\",\"PeriodicalId\":29798,\"journal\":{\"name\":\"ACS Materials Au\",\"volume\":\"5 2\",\"pages\":\"377-384\"},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2025-01-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11907284/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Materials Au\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1021/acsmaterialsau.4c00156\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2025/3/12 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Materials Au","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1021/acsmaterialsau.4c00156","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/3/12 0:00:00","PubModel":"eCollection","JCR":"Q2","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0

摘要

单原子纳米酶(SANs)是一类具有金属中心的纳米酶,模仿金属酶的结构。本文报道了模拟天然碳酸酐酶作用的Zn-N-C SAN的合成。两步退火技术导致金属含量超过18 wt %。由于金属中心作为活性位点,这种高金属负载导致了优异的催化活性。Zn-SAN的CO2吸收量为2.3 mmol/g,最终CO2转化为碳酸氢盐的转化率超过91%。通过催化剂吸附CO2进行仿生转化,然后将催化剂添加到HEPES缓冲液(pH = 8)中,开始将CO2转化为HCO3 -。之后,加入CaCl2形成白色的CaCO3沉淀,然后过滤、干燥并称重。在相同的反应条件下,以活性炭和MCM-41为对照。根据研究结果,CO2固存能力为42 mg CaCO3/mg Zn-SAN。一些对锌具有结合亲和力的氨基酸(AAs)能够通过阻断活性金属中心抑制Zn- san的酶活性。该方法可用于His、Cys、Glu和Asp的检测,检出限分别为0.011、0.031、0.029和0.062 μM,可用于商业膳食补充剂中这些原子吸收物的定量。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Zinc Single-Atom Nanozyme As Carbonic Anhydrase Mimic for CO2 Capture and Conversion.

Single-atom nanozymes (SANs) are a class of nanozymes with metal centers that mimic the structure of metalloenzymes. Herein, we report the synthesis of Zn-N-C SAN, which mimics the action of the natural carbonic anhydrase enzyme. The two-step annealing technique led to a metal content of more than 18 wt %. Since the metal centers act as active sites, this high metal loading resulted in superior catalytic activity. Zn-SAN showed a CO2 uptake of 2.3 mmol/g and a final conversion of CO2 to bicarbonate of more than 91%. CO2 was converted via a biomimetic process by allowing its adsorption by the catalyst, followed by the addition of the catalyst to HEPES buffer (pH = 8) to start the CO2 conversion into HCO3 -. Afterward, CaCl2 was added to form a white CaCO3 precipitate, which was then filtered, dried, and weighed. Active carbon and MCM-41 were used as controls under the same reaction conditions. According to the findings, the CO2 sequestration capacity was 42 mg of CaCO3/mg of Zn-SAN. Some amino acids (AAs) with binding affinity for Zn were able to suppress the enzymatic activity of Zn-SAN by blocking the active metal centers. This strategy was used for the detection of His, Cys, Glu, and Asp with detection limits of 0.011, 0.031, 0.029, and 0.062 μM, respectively, and hence was utilized for quantifying these AAs in commercial dietary supplements.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
ACS Materials Au
ACS Materials Au 材料科学-
CiteScore
5.00
自引率
0.00%
发文量
0
期刊介绍: ACS Materials Au is an open access journal publishing letters articles reviews and perspectives describing high-quality research at the forefront of fundamental and applied research and at the interface between materials and other disciplines such as chemistry engineering and biology. Papers that showcase multidisciplinary and innovative materials research addressing global challenges are especially welcome. Areas of interest include but are not limited to:Design synthesis characterization and evaluation of forefront and emerging materialsUnderstanding structure property performance relationships and their underlying mechanismsDevelopment of materials for energy environmental biomedical electronic and catalytic applications
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信