Constructing high-performance nanozymes for specific biomolecules is crucial but challenging for practical applications and fundamental research.Herein,through the examination of the catalytic reaction paths of natura...Constructing high-performance nanozymes for specific biomolecules is crucial but challenging for practical applications and fundamental research.Herein,through the examination of the catalytic reaction paths of natural nicotinamide adenine dinucleotide(NADH)oxidase(NOX),a novel and efficient single-atom rhodium catalyst(Rh1/NC)was developed to mimic NOX.The Rh_(1)/NC demonstrated the ability to catalyze the dehydrogenation of NADH and transfer electrons to O_(2)to generate H_(2)O_(2)through the typical two-electron pathway.Furthermore,our findings revealed that Rh_(1)/NC exhibits the ability to catalyze the conversion of produced H_(2)O_(2)into OH under mildly acidic conditions.This process amplifies the oxidation of NADH,showcasing NADH peroxidase-like activity(NPx-like).As a paradigm,this unique dual enzyme-like property of Rh_(1)/NC with a positive feedback effect holds significance in disrupting cancer cellular homeostasis.Rh_(1)/NC can effectively consume NADH via cascade biocatalytic reactions within cancer cells,further triggering the elevation of reactive oxygen species(ROS),leading to impaired oxidative phosphorylation and decreased mitochondrial membrane potential,thus damaging the adenosine triphosphate(ATP)synthesis.The resulting'domino effect'interferes with the energy metabolism homeostasis of cancer cells,ultimately promoting cell apoptosis.This study provides potential guidance for the rational design of materials with greater capabilities.展开更多
Most nanozyme research is limited to oxidase and peroxidase.Here,we reported the N,P,or S doped carbon nanotubes(CNTs)for enzyme mimics of nicotinamide adenine dinucleotide(NADH)oxidase and cytochrome c(Cyt c)reductas...Most nanozyme research is limited to oxidase and peroxidase.Here,we reported the N,P,or S doped carbon nanotubes(CNTs)for enzyme mimics of nicotinamide adenine dinucleotide(NADH)oxidase and cytochrome c(Cyt c)reductase.Through the doping of N element,the NADH oxidase-like activity of CNTs is highly improved,the maximum initial velocity for N doped CNT(N-CNT)is increased by 4.28 times compared to that before the modification.Through the analysis of NADH oxidation products,we found that biologically active NAD+was produced,the oxygen was selectively reduced to water or hydrogen peroxide,which is consistent with natural NADH oxidase.Furthermore,we found for the first time that carbon nanotubes can promote the transfer of electrons from NADH to Cyt c,thereby can mimic the properties of Cyt c reductase.展开更多
Recently,a study of mimic enzyme has received more attentions.However,the investigation on the oxidoreductase activity of electron mediators in the biological respiratory chain is still rare.Herein,we found that cadmi...Recently,a study of mimic enzyme has received more attentions.However,the investigation on the oxidoreductase activity of electron mediators in the biological respiratory chain is still rare.Herein,we found that cadmium sulfide(CdS)nanorods can catalyze the formation of superoxide anions.Due to the role of the photo-generated holes and the nicotinamide adenine dinucleotide(NADH)oxidation promoted by superoxide anion(O_(2)^(•−)),the CdS exhibits NADH oxidase-like activity and can be coupled with dehydrogenase to realize the recycling of NADH.It is worth mentioning that the bio-electron acceptor,cytochrome c(Cyt c),as a chromogenic substrate,can accept electrons transferred from O_(2)^(•−),which demonstrates the Cyt c reductase-like activity of CdS under physiological pH conditions.For different substrates,O_(2)^(•−)induced from CdS show oxidizing capacity for NADH and reducing capacity for Cyt c,which provides a new perspective for the in-depth study of new nanozyme.展开更多
基金financially supported by the National Natural Science Foundation of China(No.22207066)Taishan Scholars Program of Shandong Province(No.TS201712065)+2 种基金the Academic Promotion Program of Shandong First Medical University(No.2019QL009)the Science and Technology Funding from Jinan(No.2020GXRC018)the Traditional Chinese Medicine Science and Technology Project of Shandong Province(No.Q-2022142)。
文摘Constructing high-performance nanozymes for specific biomolecules is crucial but challenging for practical applications and fundamental research.Herein,through the examination of the catalytic reaction paths of natural nicotinamide adenine dinucleotide(NADH)oxidase(NOX),a novel and efficient single-atom rhodium catalyst(Rh1/NC)was developed to mimic NOX.The Rh_(1)/NC demonstrated the ability to catalyze the dehydrogenation of NADH and transfer electrons to O_(2)to generate H_(2)O_(2)through the typical two-electron pathway.Furthermore,our findings revealed that Rh_(1)/NC exhibits the ability to catalyze the conversion of produced H_(2)O_(2)into OH under mildly acidic conditions.This process amplifies the oxidation of NADH,showcasing NADH peroxidase-like activity(NPx-like).As a paradigm,this unique dual enzyme-like property of Rh_(1)/NC with a positive feedback effect holds significance in disrupting cancer cellular homeostasis.Rh_(1)/NC can effectively consume NADH via cascade biocatalytic reactions within cancer cells,further triggering the elevation of reactive oxygen species(ROS),leading to impaired oxidative phosphorylation and decreased mitochondrial membrane potential,thus damaging the adenosine triphosphate(ATP)synthesis.The resulting'domino effect'interferes with the energy metabolism homeostasis of cancer cells,ultimately promoting cell apoptosis.This study provides potential guidance for the rational design of materials with greater capabilities.
基金the National Key Research and Development Program of China(No.2019YFA0709202)Natural Science Foundation of Jilin Province(No.20220101055JC)+1 种基金the International Cooperation Project of Jilin Scientific and Technological Development Program(No.20190701059GH)the National Natural Science Foundation of China(No.31301177).
文摘Most nanozyme research is limited to oxidase and peroxidase.Here,we reported the N,P,or S doped carbon nanotubes(CNTs)for enzyme mimics of nicotinamide adenine dinucleotide(NADH)oxidase and cytochrome c(Cyt c)reductase.Through the doping of N element,the NADH oxidase-like activity of CNTs is highly improved,the maximum initial velocity for N doped CNT(N-CNT)is increased by 4.28 times compared to that before the modification.Through the analysis of NADH oxidation products,we found that biologically active NAD+was produced,the oxygen was selectively reduced to water or hydrogen peroxide,which is consistent with natural NADH oxidase.Furthermore,we found for the first time that carbon nanotubes can promote the transfer of electrons from NADH to Cyt c,thereby can mimic the properties of Cyt c reductase.
基金supported by the National Key R&D Program of China(No.2019YFA0709202)MOST China(No.2016YFA0203200)+1 种基金the International Cooperation Project of Jilin Scientific and Technological Development Program(No.20190701059GH)the National Natural Science Foundation of China(Nos.21721003 and 31301177).
文摘Recently,a study of mimic enzyme has received more attentions.However,the investigation on the oxidoreductase activity of electron mediators in the biological respiratory chain is still rare.Herein,we found that cadmium sulfide(CdS)nanorods can catalyze the formation of superoxide anions.Due to the role of the photo-generated holes and the nicotinamide adenine dinucleotide(NADH)oxidation promoted by superoxide anion(O_(2)^(•−)),the CdS exhibits NADH oxidase-like activity and can be coupled with dehydrogenase to realize the recycling of NADH.It is worth mentioning that the bio-electron acceptor,cytochrome c(Cyt c),as a chromogenic substrate,can accept electrons transferred from O_(2)^(•−),which demonstrates the Cyt c reductase-like activity of CdS under physiological pH conditions.For different substrates,O_(2)^(•−)induced from CdS show oxidizing capacity for NADH and reducing capacity for Cyt c,which provides a new perspective for the in-depth study of new nanozyme.
