Electron transfer and interfacial behavior of redox proteins

Zhou, Nandi; Cao, Ya; Li, Genxi

doi:10.1007/s11426-010-0134-8

Cited by 6 publications

(4 citation statements)

References 141 publications

(153 reference statements)

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“…Changes in the composition and content of the interfacial redox mediators or terminal electron transfer proteins may influence the interfacial electron transfer rate. , The shape of the non-turnover CV on the 3rd day was similar to that of the well-known exoelectrogens Geobacter . , The redox peak that appeared was related to the redox behavior of Geobacter’s cytochrome C on the electrode surface. There were several vital cytochromes C in Geobacter responsible for EET, including OmcS, OmcZ, and OmcB, with a redox potential of −0.36 V. , The non-turnover CV on the 3rd day had four groups of redox peaks (Figure A).…”

Section: Resultsmentioning

confidence: 83%

“…30 Changes in the composition and content of the interfacial redox mediators or terminal electron transfer proteins may influence the interfacial electron transfer rate. 31,32 The shape of the non-turnover CV on the 3rd day was similar to that of the well-known exoelectrogens Geobacter. 33,34 The redox peak that appeared was related to the redox behavior of Geobacter's cytochrome C on the electrode surface.…”

Section: Response Of Cathodic Current and Nitratementioning

confidence: 99%

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Unveiling the Mechanism of Enhanced Extracellular Electron Transfer by Polarity Inversion of Bioelectrodes

et al. 2022

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Polarity inversion from the bioanode to the biocathode enables a rapid formation of efficient biofilms for microbial electrochemical reduction. Though this approach has been widely adopted for various applications, the mechanism behind the enhanced extracellular electron transfer (EET) during the polarity inversion process remains unclear. Therefore, in this study, the succession pattern and electron transfer mechanism of the inverted denitrifying biocathode were investigated by continuously monitoring the electrochemical properties, denitrification dynamics, and biofilm characteristics. The results indicated that the highest current density of the biocathode after inversion from bioanode was twice that of the steady current density, and the dominant flora of the electrode biofilm shifted from Geobacter sp. to denitrifying bacteria (e.g., Shinella and Comamonas). The reversal polarity induced a decreasing content of cytochrome C, while iron-containing compounds were found to be responsible for an enhanced EET within the denitrification process. This study provides a deep understanding of the EET mechanism behind the electrode polarity inversion and is of great significance for the future development of biocathode applications.

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Section: Resultsmentioning

confidence: 83%

Section: Response Of Cathodic Current and Nitratementioning

confidence: 99%

Unveiling the Mechanism of Enhanced Extracellular Electron Transfer by Polarity Inversion of Bioelectrodes

et al. 2022

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“…The reduction was carried out due to the reaction of PCB29 with active hydrogen stored on the electrode surface. The process was a direct electrochemical reduction [17][18][19], which could be explained by further electrode reaction controlled by adsorption process within the scan rate range [20,21]. Laviron equation [22] is used for the quantitative relationship of the reaction which is not controlled by diffusion in the solution.…”

Section: Electrochemical Performance Of the Pd/ti Electrodementioning

confidence: 99%

Preparation and electrocatalytic dechlorination performance of Pd/Ti electrode

Zhang

Cao

Chi

et al. 2014

Desalination and Water Treatment

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A B S T R A C TThe Pd/Ti working electrode was prepared by the electrochemical deposition on the Ti plate and its structure and morphology were analyzed by an X-ray diffraction (XRD) and a transmission electron microscopy. The results showed that Palladium (Pd) crystals were coated uniformly on Titanium (Ti) base material with the average size of 8.69 nm. The cyclic voltammetry was employed to study the electrochemical reduction characteristics of 2,4,5-tripolychlorinated biphenyl (PCB29) in an electrocatalytic system. The results showed that the PCB29 dechlorination was a two-electron transfer reduction controlled by adsorption and conformed to the characteristics of the first-order reaction. The efficiencies of PCB29 degradation in the electrocatalytic system were more than 95% after 5 h at its concentration (mg/L) of 60, 80, and 100. The dechlorinations of PCB29 obeyed the pseudo-first-order reaction kinetic behavior. The reaction rate constant was approximately 0.011 min −1 . The reaction rate increased slightly as the temperature rose. The 2,5-PCB was first mainly generated by PCB29 para-position dechlorination, 2-PCB by meta-position dechlorination, and then diphenyl by the subsequent ortho-position dechlorination. Diphenyl could be further hydrogenated to phenyl cyclohexane. The chlorine substitution position on PCB29 mainly affected the order of PCB29 electrocatalytic dechlorination.

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“…10 Recently, several nanomaterials, including carbon nanotube (CNT), and nanoparticles of Au, Ag, TiO2, Fe3O4 or MnO2, have been applied to electrochemical studies of redox protein. [11][12][13][14] Native proteins or enzymes are usually not suitable to be used directly in industrial, agricultural, medical and other fields because of their expensive price, difficulty to gain, instability or incapacity to work under different conditions. The designs of heme proteins have recently become an active area of research.…”

Section: Introductionmentioning

confidence: 99%

A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode

et al. 2012

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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.

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Electron transfer and interfacial behavior of redox proteins

Cited by 6 publications

References 141 publications

Unveiling the Mechanism of Enhanced Extracellular Electron Transfer by Polarity Inversion of Bioelectrodes

Unveiling the Mechanism of Enhanced Extracellular Electron Transfer by Polarity Inversion of Bioelectrodes

Preparation and electrocatalytic dechlorination performance of Pd/Ti electrode

A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode

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