Square‐Wave Voltammetry: A Review on the Recent Progress

Mirčeski, Valentin; Gulaboski, Rubin; Lovrić, Milivoj; Bogeski, Ivan; Kappl, Reinhard; Hoth, Markus

doi:10.1002/elan.201300369

Cited by 196 publications

(171 citation statements)

References 146 publications

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“…The first voltammetric pair of peaks corresponds to the creation of a stable radical cation of ABTS, the second oxidation step to formation of a di-cation of ABTS. Both signals in the cyclic voltammograms of ABTS can be described as one-electron diffusion controlled redox processes [35], because cyclic voltammograms of ABTS recorded at different scan rates show two well-defined peaks characterized by peak-to-peak separations of about 60 mV (Fig. S7).…”

Section: Antioxidative Potential Of the Hydroxyl Derivatives Of Coenzmentioning

confidence: 99%

New insights into the chemistry of Coenzyme Q-0: A voltammetric and spectroscopic study

Gulaboski

Bogeski

Kokoškarova

et al. 2016

Bioelectrochemistry

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Coenzyme Q-0 (CoQ-0) is the only Coenzyme Q lacking an isoprenoid group on the quinoid ring, a feature important for its physico-chemical properties. Here, the redox behavior of CoQ-0 in buffered and non-buffered aqueous media was examined. In buffered aqueous media CoQ-0 redox chemistry can be described by a 2-electron-2-proton redox scheme, characteristic for all benzoquinones. In non-buffered media the number of electrons involved in the electrode reaction of CoQ-0 is still 2; however, the number of protons involved varies between 0 and 2. This results in two additional voltammetric signals, attributed to 2-electrons-1H + and 2-electrons-0H + redox processes, in which mono-and di-anionic compounds of CoQ-0 are formed. In addition, CoQ-0 exhibits a complex chemistry in strong alkaline environment. The reaction of CoQ-0 and OH − anions generates several hydroxyl derivatives as products. Their structures were identified with HPLC/MS. The prevailing radical reaction mechanism was analyzed by electron paramagnetic resonance spectroscopy. The hydroxyl derivatives of CoQ-0 have a strong antioxidative potential and form stable complexes with Ca 2+ ions. In summary, our results allow mechanistic insights into the redox properties of CoQ-0 and its hydroxylated derivatives and provide hints on possible applications.

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Section: Antioxidative Potential Of the Hydroxyl Derivatives Of Coenzmentioning

confidence: 99%

New insights into the chemistry of Coenzyme Q-0: A voltammetric and spectroscopic study

Gulaboski

Bogeski

Kokoškarova

et al. 2016

Bioelectrochemistry

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“…A lot of theoretical features of the EC (electrochemicalchemical), CE (chemical-electrochemical), ECE (electrochemicalchemical-electrochemical), EC' (electrochemical-catalytic) systems under voltammetric conditions at various electrodes are appropriately elaborated in several excellent books [1][2][3][4][5][6], theoretical studies and reviews [7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26]. The so-called electrocatalytic regenerative mechanism (often referred to as EC' or ECat mechanism) is one of the most intriguing from a theoretical point of view, since it differs in many aspects from the other three mechanisms (EC, CE, and ECE) [1,[5][6][7][8]11,13,16,[18][19][20][21][22][23][24][25][26]. The EC' electrode mechanism comprises regeneration of the initial electroactive species involved in the electrode reaction via homogeneous redox reaction of the electrochemically generated product with other redox species present in the electrolyte solution.…”

Section: Introductionmentioning

confidence: 99%

New aspects of the electrochemical-catalytic (EC’) mechanism in square-wave voltammetry

Gulaboski

Mirčeski

2015

Electrochimica Acta

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Keywords:EC' catalytic mechanism electrode reaction kinetics standard rate constant enzymatic biosensors protein-film voltammetry A B S T R A C T Several new theoretical aspects of the electrocatalytic (regenerative) EC' mechanism under conditions of square-wave (SWV) and staircase cyclic voltammetry (SCV) are presented. Elaborating the effect of the rate of the catalytic reaction in the diffusion-controlled catalytic mechanism (diffusional EC' mechanism) and surface catalytic mechanism (surface EC' mechanism), we refer to several phenomena related to the shift of the position and the half-peak width of the net peak in square-wave voltammetry (SWV). If the rate of the catalytic reaction is much higher than the kinetics of the electrode reaction, a linear dependence between the peak potential of the simulated net SWV peaks and the logarithm of the catalytic parameter can be observed. The intercept of that linear dependence is a function of the kinetics of the electrode reaction. Based on this finding, we propose a new methodology to determine the electrode kinetics rate constant. The proposed approach relies on the variation of the concentration of the regenerative reagent. To the best of our knowledge, this is one of very few voltammetric approaches for electrode kinetic measurements not based on the time or potential variation in the experimental analyzes. In addition, we present a brief analysis of the catalytic mechanism under conditions of staircase cyclic voltammetry in order to emphasize the main differences between SCV and SWV.

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“…1 partly modified with the organic solution droplet containing the redox probe only. In order to increase the sensitivity and precision of the voltammetric measurements, square-wave voltammetry has been utilized [47]. The role of the enzyme was studied at pH 4.5 and 5.6.…”

Section: Resultsmentioning

confidence: 99%

Studying the ion transfer across liquid interface of thin organic-film-modified electrodes in the presence of glucose oxidase

Mirčeski

Mitrova

Ivanovski

et al. 2015

J Solid State Electrochem

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A coupled electron-ion transfer reaction at thin organic-film-modified electrodes (TFE) is studied in the presence of glucose oxidase (GOx) under voltammetric conditions. TFE consists of a graphite electrode modified with a nitrobenzene solution of decamethylferrocene (DMFC) as a redox mediator and tetrabuthylammonium perchlorate as an organic-supporting electrolyte, in contact with aqueous buffer solutions containing percholarte ions and GOx. The redox turnover of DMFC coupled with perchlorate transfer across water|nitrobenzene interface composes the coupled electronion transfer reaction. Glucose oxidase strongly adsorbs at the liquid|liquid interface affecting the coupled electron-ion transfer reaction by reducing the surface area of the liquid interface, prompting coadsorption of the transferring ion and lowering down slightly the rate of the ion transfer reaction. Although the enzyme exists as a polyvalent anion over the pH interval from 5.6 to 7, it does not participate directly in the ionic current across the liquid interface and percholrate remains the main transferring ion. Raman spectroscopic data, together with the voltammetric data collected by three-phase droplet electrodes, indicate that the adsorption of the enzyme does not depend either on the redox mediator (DMFC) or the organicsupporting electrolyte, while being driven by intrinsic interactions of the enzyme with the organic solvent. The overall electrochemical mechanism is mathematically modeled by considering linear adsorption isotherm of the transferring ion, semi-infinite mass transfer regime, and phenomenological second-order kinetic model.

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Square‐Wave Voltammetry: A Review on the Recent Progress

Cited by 196 publications

References 146 publications

New insights into the chemistry of Coenzyme Q-0: A voltammetric and spectroscopic study

New insights into the chemistry of Coenzyme Q-0: A voltammetric and spectroscopic study

New aspects of the electrochemical-catalytic (EC’) mechanism in square-wave voltammetry

Studying the ion transfer across liquid interface of thin organic-film-modified electrodes in the presence of glucose oxidase

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