Electrochemical stability of catechols with a pyrene side chain strongly adsorbed on graphite electrodes for catalytic oxidation of dihydronicotinamide adenine dinucleotide

Jaegfeldt, Hans; Kuwana, Theodore; Johansson, Gillis

doi:10.1021/ja00345a021

Cited by 301 publications

(162 citation statements)

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“…One of the most attractive electrode elements for a potentially implantable BFC is a carbon material, which is cheap, abundant and biocompatible. To design this BFC, SPGE were chosen, as such electrodes are well-characterised [30] and widely used for bioelectrochemical studies of variety of enzymes including different CDH [17,28,31,32] and BOx [20,29], on which both bioelements showed excellent DET-based bioelectrocatalysis (Figures 2 and 3).…”

Section: Resultsmentioning

confidence: 99%

A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

et al. 2010

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We report on the fabrication and characterisation of the very first direct electron transfer‐based glucose/oxygen biofuel cell (BFC) operating in neutral glucose‐containing buffer and human serum. Corynascus thermophilus cellobiose dehydrogenase and Myrothecium verrucaria bilirubin oxidase were used as anodic and cathodic bioelements, respectively. The following characteristics of the mediator‐, separator‐ and membrane‐less, a priori, non‐toxic and simple miniature BFC, was obtained: an open‐circuit voltage of 0.62 and 0.58 V, a maximum power density of ca. 3 and 4 μW cm–2 at 0.37 and 0.19 V of cell voltage, in phosphate buffer and human serum, respectively.

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Section: Resultsmentioning

confidence: 99%

A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

et al. 2010

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“…This number is significantly higher than the theoretical monolayer enzyme coverage estimated on the basis of the molecular dimensions of HMP (Ilari et al, 2002) as 3-5.5 pmol cm À 2 (depending on the enzyme orientation). Considering the high surface roughness of the Gr electrodes used (the roughness factor above 5 (Jaegfeldt et al, 1983)), the HMP coverage corrected for the real electrode surface area decreases to 100 pmol cm À 2 , which is still unusually high. It suggests that the majority of the FAD voltammetric signal is likely to originate from FAD released from HMP due to protein unfolding.…”

Section: Direct Electrochemistry Of Hmp Adsorbed On Graphitementioning

confidence: 97%

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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“…In spite of the fact that SPGE is well-characterized [57] and widely used for MCO studies [39,79,80], it is not a very good electrode for fundamental bioelectrochemical investigations of redox proteins.…”

Section: Myrothecium Verrucaria Boxmentioning

confidence: 99%

On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

et al. 2012

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The catalytic cycle of multicopper oxidases (MCOs) involves intramolecular electron transfer (IET) from the Cu‐T1 copper ion, which is the primary site of the one‐electron oxidations of the substrate, to the trinuclear copper cluster (TNC), which is the site of the four‐electron reduction of dioxygen to water. In this study we report a detailed characterization of the kinetic and electrochemical properties of bilirubin oxidase (BOx) – a member of the MCO family. The experimental results strongly indicate that under certain conditions, e.g. in alkaline solutions, the IET can be the rate‐limiting step in the BOx catalytic cycle. The data also suggest that one of the catalytically relevant intermediates (most likely characterized by an intermediate oxidation state of the TNC) formed during the catalytic cycle of BOx has a redox potential close to 0.4 V, indicating an uphill IET process from the T1 copper site (0.7 V) to the Cu‐T23. These suggestions are supported by calculations of the IET rate, based on the experimentally observed Gibbs free energy change and theoretical estimates of reorganization energy obtained by combined quantum and molecular mechanical (QM/MM) calculations.

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Electrochemical stability of catechols with a pyrene side chain strongly adsorbed on graphite electrodes for catalytic oxidation of dihydronicotinamide adenine dinucleotide

Cited by 301 publications

References 1 publication

A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

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

On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

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