An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration

Mak, K. K.; Wollenberger, Ulla; Scheller, Frieder W.; Renneberg, Reinhard

doi:10.1016/s0956-5663(02)00245-2

Cited by 48 publications

(25 citation statements)

References 21 publications

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“…Over 400 NAD(P) þ -dependent dehydrogenases use NAD (P) þ as the electron acceptor recycling the enzyme after reaction with the substrate (Gorton and Domínguez, 2007;Lobo et al, 1997), and these biocatalytic reactions find wide applications in electrochemical biosensors (Gorton and Domínguez, 2007;Lobo et al, 1997;Maka et al, 2003) and biofuel cell development (Minteer et al, 2007). Therewith, it is crucial that NAD(P)H produced during the biocatalytic cycle can be electrochemically regenerated.…”

Section: Introductionmentioning

confidence: 99%

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: Introductionmentioning

confidence: 99%

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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“…LBL (layer-bylayer) will be marking technique, allows to the amounts enzyme catalytic activity to an increase in the signal , Zhao and Ju, 2006. On the other hand the connection of multi-layer enzyme dramatically increases the analytical signal (Limoges et al, 2008;Limoges et al, 2006, Bauer et al, 1996Schelde et al, 2001and Mak et al, 2003, Kwon et al, 2008. Primarily on the preparation of SWCNT multienzyme LBL layer was prepared by modification of immunosensor (Munge et al, 2005, Zhou and.…”

Section: Electrochemical Immunosensors Developed For the Detection Ofmentioning

confidence: 99%

Biosensors for Cancer Biomarkers

Uygun¹,

Sezgintürk²

2011

Biosensors - Emerging Materials and Applications

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“…To preserve its activity, the immobilized enzyme should retain its native conformation. Various methods such as adsorption, covalent binding using bifunctional reagents [24], physical entrapment in a polymer matrix [25], self assembled monolayer (SAM) [6], or Langmuir-Blodgett films [26] have been used to immobilize enzymes onto the surface of different transducers. Since the analytical performances of the biosensor are strongly affected by these processes, intensive efforts need to be done in order to develop successful immobilization procedures.…”

Section: Introductionmentioning

confidence: 99%

Metal chelate affinity to immobilize horseradish peroxidase on functionalized agarose/CNTs composites for the detection of catechol

Luo

et al. 2011

Sci. China Chem.

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The paper reports a novel amperometric biosensor for catechol based on immobilization of a highly sensitive horseradish peroxidase by affinity interactions on metal chelate-functionalized agarose/carbon nanotubes composites. Metal chelate affinity takes advantage of the affinity of Ni 2+ ions to bind strongly and reversibly to histidine or cysteine tails found on the surface of the horseradish peroxidase. Thus, enzymes with such residues in their molecules can be easily attached to functionalized agarose/carbon nanotubes composites support containing a nickel chelate. Linear sweep voltammograms and amperometry are used to study the proposed electrochemical biosensor. Catechol is determined by direct reduction of biocatalytically liberated quinone species at −0.05 V (vs. SCE). The effect of pH, applied electrode potential and the concentration of H 2 O 2 on the sensitivity of the biosensor has been investigated. The performance of the proposed biosensor is tested using four different phenolic compounds, showing very high sensitivity, in particular, the linearity of catechol is observed from 2.0 × 10 −8 to 1.05 × 10 −5 M with a detection limit of 5.0 × 10 −9 M. amperometric biosensor, carbon nanotubes, metal chelation, agarose, catechol

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An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration

Cited by 48 publications

References 21 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

Biosensors for Cancer Biomarkers

Metal chelate affinity to immobilize horseradish peroxidase on functionalized agarose/CNTs composites for the detection of catechol

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