A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode
A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluste...
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| Published in | Analytical Sciences Vol. 28; no. 7; pp. 711 - 716 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Singapore
The Japan Society for Analytical Chemistry
2012
Springer Nature Singapore Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0910-6340 1348-2246 1348-2246 |
| DOI | 10.2116/analsci.28.711 |
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| Abstract | A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis–Menten (Km) and catalytic rate (kcat) constants of the AP were determined to be 2.5 ± 0.4 μM and 0.069 ± 0.001 s−1, respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 μM−1 s−1, which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°′) of –45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (ks) was evaluated to be 0.65 s−1. The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10−10 mol cm−2. The apparent Michaelis–Menten constant (Kmapp) was 0.23 nM. |
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| AbstractList | A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis–Menten (Km) and catalytic rate (kcat) constants of the AP were determined to be 2.5 ± 0.4 μM and 0.069 ± 0.001 s−1, respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 μM−1 s−1, which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°′) of –45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (ks) was evaluated to be 0.65 s−1. The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10−10 mol cm−2. The apparent Michaelis–Menten constant (Kmapp) was 0.23 nM. A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c ). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten ( K m ) and catalytic rate ( k cat ) constants of the AP were determined to be 2.5 ± 0.4 µM and 0.069 ± 0.001 s −1 , respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 µM −1 s −1 , which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential ( E°′ ) of −45 ± 2 mV ( vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant ( k s ) was evaluated to be 0.65 s −1 . The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10 −10 mol cm −2 . The apparent Michaelis-Menten constant ( K m app ) was 0.23 nM. A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (K(m)) and catalytic rate (k(cat)) constants of the AP were determined to be 2.5 ± 0.4 µM and 0.069 ± 0.001 s(-1), respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 µM(-1) s(-1), which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°') of -45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (k(s)) was evaluated to be 0.65 s(-1). The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10(-10) mol cm(-2). The apparent Michaelis-Menten constant (K(m)(app)) was 0.23 nM.A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (K(m)) and catalytic rate (k(cat)) constants of the AP were determined to be 2.5 ± 0.4 µM and 0.069 ± 0.001 s(-1), respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 µM(-1) s(-1), which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°') of -45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (k(s)) was evaluated to be 0.65 s(-1). The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10(-10) mol cm(-2). The apparent Michaelis-Menten constant (K(m)(app)) was 0.23 nM. A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (Km) and catalytic rate (kcat) constants of the AP were determined to be 2.5 +/- 0.4 mu M and 0.069 +/- 0.001 s-1, respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 +/- 0.005 mu M-1 s-1, which was 39 +/- 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E degree ') of -45 +/- 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (ks) was evaluated to be 0.65 s-1. The surface concentration of electroactive AP on GC electrode ( gamma ) was 7 x 10-10 mol cm-2. The apparent Michaelis-Menten constant (Kmapp) was 0.23 nM. A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (Km) and catalytic rate (kcat) constants of the AP were determined to be 2.5 ± 0.4 μM and 0.069 ± 0.001 s-1, respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 μM-1 s-1, which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°') of -45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (ks) was evaluated to be 0.65 s-1. The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10-10 mol cm-2. The apparent Michaelis-Menten constant (Kmapp) was 0.23 nM. A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (K(m)) and catalytic rate (k(cat)) constants of the AP were determined to be 2.5 ± 0.4 µM and 0.069 ± 0.001 s(-1), respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 µM(-1) s(-1), which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°') of -45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (k(s)) was evaluated to be 0.65 s(-1). The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10(-10) mol cm(-2). The apparent Michaelis-Menten constant (K(m)(app)) was 0.23 nM. |
| Author | HUANG, Kun XIAO, Bao-Lin GAO, Yun-Fei MOOSAVI-MOVAHEDI, Ali Akbar YANG, Wei-Yun HONG, Jun GHOURCHIAN, Hedayatollah WANG, Wei ZHAO, Ying-Xue MOOSAVI-MOVAHEDI, Zainab |
| Author_xml | – sequence: 1 fullname: YANG, Wei-Yun organization: College of Life Science, Henan University – sequence: 1 fullname: GAO, Yun-Fei organization: College of Life Science, Henan University – sequence: 1 fullname: XIAO, Bao-Lin organization: College of Life Science, Henan University – sequence: 1 fullname: ZHAO, Ying-Xue organization: College of Life Science, Henan University – sequence: 1 fullname: MOOSAVI-MOVAHEDI, Zainab organization: Chemistry & Chemical Engineering Research Center of Iran (CCERCI) – sequence: 1 fullname: WANG, Wei organization: College of Life Science, Henan University – sequence: 1 fullname: MOOSAVI-MOVAHEDI, Ali Akbar organization: Institute of Biochemistry and Biophysics, University of Tehran – sequence: 1 fullname: HUANG, Kun organization: College of Life Science, Henan University – sequence: 1 fullname: HONG, Jun organization: College of Life Science, Henan University – sequence: 1 fullname: GHOURCHIAN, Hedayatollah organization: Institute of Biochemistry and Biophysics, University of Tehran |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22790375$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_3390_ma16196500 crossref_primary_10_1155_2014_480498 crossref_primary_10_1007_s13738_014_0410_1 crossref_primary_10_1016_j_bej_2022_108463 crossref_primary_10_1007_s11368_020_02741_w crossref_primary_10_1007_s13738_015_0756_z crossref_primary_10_1016_j_pbiomolbio_2018_03_001 crossref_primary_10_1016_j_electacta_2012_11_054 crossref_primary_10_1016_j_molliq_2018_12_011 |
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| Snippet | A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission... A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c ). UV-Vis spectrometry and transmission... |
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| SubjectTerms | Analytical Chemistry Animals Biomimetic Materials - chemistry Biomimetic Materials - metabolism Biosensing Techniques Carbon Catalysts Chemistry Constants Cytochromes c - metabolism Electrochemistry Electrochemistry - instrumentation Electrochemistry - methods Electrodes Fluorocarbon Polymers - chemistry Glass - chemistry Glassy carbon Gold - chemistry Hydrogen Peroxide - analysis Hydrogen-Ion Concentration Kinetics Limit of Detection Membranes, Artificial Metal Nanoparticles - chemistry Nanocomposites Nanomaterials Nanostructure Nanostructures - chemistry Nanotubes, Carbon - chemistry Peroxidase Peroxidase - metabolism Spectrometry |
| Title | A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode |
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