{"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}
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.
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