Regulation of graphdiyne-based nanozymes with enhanced oxidaselike activity by cobalt and nitrogen codoping
作者机构:CAS Key Laboratory for Biomedical Effects of Nanomaterial&NanosafetyInstitute of High Energy PhysicsChinese Academy of ScienceBeijing 100049China Key Laboratory of Functional Inorganic Material ChemistryMinistry of EducationSchool of Chemistry and Materials ScienceHeilongjiang UniversityHarbin 150080China Laboratory of Theoretical and Computational NanoscienceNational Center for Nanoscience and TechnologyBeijing 100190China University of Chinese Academy of SciencesBeijing 100049China
出 版 物:《Nano Research》 (纳米研究(英文版))
年 卷 期:2025年第18卷第1期
页 面:21-29页
核心收录:
学科分类:081704[工学-应用化学] 07[理学] 070304[理学-物理化学(含∶化学物理)] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学]
基 金:supported financially by the National Key Research and Development Program of China(Nos.2022YFA1205900 and 2018YFA0703504) the Directional Institutionalized Scientific Research Platform relied on Beijing Synchrotron Radiation Facility of Chinese Academy of Sciences
主 题:nanozymes oxidase-like activity graphdiyne heteroatom doping regulation
摘 要:The development of nanozymes with excellent intrinsic oxidase-like activity and specificity has received increasing ***(GDY)could be a promising choice for designing nanozymes with enhanced oxidase(OXD)-like activity due to its unique structure and ***,Co-N-GDY with high OXD activity but no peroxidase(POD)activity was synthesized by codoping of cobalt(Co)and nitrogen(N)into GDY and compared with other GDY-based nanozymes(including GDY,Co-GDY,and N-GDY).Upon analyzing the doping effect of Co and N on the OXD-like and POD-like activities,we found that the combination of Co and N in GDY played a significant role in enhancing the OXD-like activity,and even reversed the POD-like activity of N-GDY to OXD-like activity of *** electrochemical experiment and the theoretical calculations provided an explanation for the mechanism and showed that the activity was closely linked to the reduction ability of O_(2) or H_(2)O_(2) on the nanozyme substrates,which was determined by the ratedetermining step of the catalytic reaction.