Interaction of Flavin Adenine Dinucleotide (FAD) with a Glassy Carbon Electrode Surface

Wei, Hai-Zhen; Omanovic, Sasha

doi:10.1002/cbdv.200890150

Cited by 32 publications

(48 citation statements)

References 33 publications

(42 reference statements)

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“…The peak potentials in CV and DPV linearly depended on pH with a slope of À 60 77 mV per pH unit (Fig. S2, ESI), indicating an equal number of protons and electrons involved in the redox process (Bard and Faulkner, 1980) in consistence with other reports on the electrochemistry of FAD/ FADH 2 (Gorton and Johansson, 1980;Wei and Omanovic, 2008). The analysis of the full peak width at the half-peak height for a cathodic and anodic process (Laviron, 1979) at low scan rates confirmed a 2e À transformation of the FAD/FADH 2 couple with the transfer coefficient a of 0.42.…”

Section: Direct Electrochemistry Of Hmp Adsorbed On Graphitesupporting

confidence: 83%

Direct electrochemistry and Os-polymer-mediated bioelectrocatalysis of NADH oxidation by Escherichia coli flavohemoglobin at graphiteelectrodes

Sosna

Bonamore²,

Gorton

et al. 2013

Biosensors and Bioelectronics

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a b s t r a c tEscherichia coli flavohemoglobin (HMP), which contains one heme and one FAD as prosthetic groups and is capable of reducing O 2 by its heme at the expense of NADH oxidized at its FAD site, was electrochemically studied at graphite (Gr) electrodes. Two signals were observed in voltammograms of HMP adsorbed on Gr, at À 477 and À 171 mV vs. Ag9AgCl, at pH 7.4, correlating with electrochemical responses from the FAD and heme domains, respectively. The electron transfer rate constant for ET reaction between FAD of HMP and the electrode was estimated to be 83 s. Direct bioelectrocatalytic oxidation of NADH by HMP was not observed, presumably due to impeded substrate access to HMP orientated on Gr through the FAD-domain and/or partial denaturation of HMP. Bioelectrocatalysis was achieved when HMP was wired to Gr by the Os redox polymers, with the onset of NADH oxidation at the formal potential of the particular Os complex (þ140 mV or À 195 mV). Apparent Michaelis constants K M app and j max were determined, showing bioelectrocatalytic efficiency of NADH oxidation by HMP exceeding the one earlier shown with diaphorase, which makes HMP very attractive as a component of bioanalytical and bioenergetic devices.

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Section: Direct Electrochemistry Of Hmp Adsorbed On Graphitesupporting

confidence: 83%

Direct electrochemistry and Os-polymer-mediated bioelectrocatalysis of NADH oxidation by Escherichia coli flavohemoglobin at graphiteelectrodes

Sosna

Bonamore²,

Gorton

et al. 2013

Biosensors and Bioelectronics

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“…Free FAD gave a peak at ca. À0.315 V [25] and the shift of formal potential with pH was close to 0.059 (curve 6, Figure 2B) The three other signals observed did not show a strict dependence on pH, so they are most probably connected with heme c sites. The E vs. pH relationship displayed a region where the proton coupling to heme oxidation/reduction processes was evident.…”

Section: Resultsmentioning

confidence: 89%

Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Kizling

Bilewicz

2017

ChemElectroChem

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We present kinetic and mechanistic studies of fructose oxidation by fructose dehydrogenase (FDH) using the electrochemical methods of stationary and rotating disk voltammetry. FDH was physically adsorbed on unmodified multiwalled carbon nanotubes (MWCNT) to study direct electron transfer (DET) parameters, and for comparison an MWCNT with an adsorbed pyrene derivative of naphthoquinone employed as the mediator in mediated electron transfer, MET, was also examined. Kinetic parameters, such as the number of electrons transferred, the turnover number, and the electron transfer rate constant, were calculated. Comparison of the non-turnover and catalytic behaviour revealed the role of the heme c active site in the electron transfer of FDH. It was also shown that a mediator with a sufficiently low formal potential, such as the naphthoquinone, substitutes for the heme c site in the electron transfer to the electrode. The kinetic parameters of the processes proved that the application of the mediator results in an increase in the rate of fructose catalytic oxidation compared to that of the DET oxidation process.

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“…3B, black line) and compared with the CV of the MWCNT/PyBA-AOx film. The CV of the MWCNT/PyBA-FAD electrode indicated a pair of redox peaks with E pa = À0.461 V and E pc = À0.455 V with the formal potential calculated to be E 0 = À0.458 V which is similar to the standard reduction potential (À0.200 V vs. NHE) for the FAD/FADH 2 redox couple [15] and close to E 0 = À0.464 V estimated for the FAD cofactor deposited on GCE [24]. The peak width at half height (E fwhm ) was calculated to be 75 mV, which is higher than the theoretical value for one-or two-electron processes [25].…”

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confidence: 87%

Bioelectrocatalytic Activity of Immobilized Alcohol Oxidase on 4‐(pyrrole‐1‐yl) Benzoic Acid Modified Carbon Nanotubes

Kowalewska

Jakubow

2016

Electroanalysis

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A novel bioelectrocatalytic system was prepared by immobilizing alcohol oxidase (AOx) onto multiwalled carbon nanotubes (MWCNT) modified with 4‐(pyrrole‐1‐yl) benzoic acid (PyBA). Functional carboxylic groups from PyBA create covalent amide linkages with amine groups from the enzyme molecule and provide an anchor for the effective immobilization of AOx improving the stability of the whole system. The immobilized enzyme displayed a pair of reversible redox peaks of flavin adenine dinucleotide (FAD) cofactor with the formal potential E0’=−0.451 V. The response showed a surface‐controlled electrode process with the heterogeneous electron transfer rate constant ks=2.7 s−1. Under aerobic conditions AOx(FADH2) can be oxidized to AOx(FAD) by oxygen, which then reacts with ethanol decreasing the cathodic response, which could be used for ethanol detection with a high sensitivity 13.1 μA mM−1 cm−2. The lack of bioactivity towards ethanol in anaerobic conditions suggests the presence of two types of AOx molecules in the system: active with oxygen maintaining the direct electron transfer feature and not active without a redox mediator, due to the deeply embedded FAD cofactor. The polarization curve showed that the electrooxidation current of ethanol appears at −410 mV and reaches 2.0 µA cm−1 at −300 mV. In this case, the bioactivity of AOx to ethanol can be observed offering promising solution for the development of mediatorless systems for application to biosensors and biofuel cells.

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Interaction of Flavin Adenine Dinucleotide (FAD) with a Glassy Carbon Electrode Surface

Cited by 32 publications

References 33 publications

Direct electrochemistry and Os-polymer-mediated bioelectrocatalysis of NADH oxidation by Escherichia coli flavohemoglobin at graphiteelectrodes

Direct electrochemistry and Os-polymer-mediated bioelectrocatalysis of NADH oxidation by Escherichia coli flavohemoglobin at graphiteelectrodes

Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Bioelectrocatalytic Activity of Immobilized Alcohol Oxidase on 4‐(pyrrole‐1‐yl) Benzoic Acid Modified Carbon Nanotubes

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