A fully active monolayer enzyme electrode derivatized by antigen-antibody attachment

Bourdillon, Christian; Demaille, Christophe; Guéris, J; Moiroux, Jacques; Savéant, Jean Michel

doi:10.1021/ja00079a005

Cited by 213 publications

(227 citation statements)

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“…This makes a complexation of the cations with the glucose oxidase active center plausible. The possibility of complex formation of glucose oxidase with oxidized ferrocenes was also hypothesized in a very recent publication by Bourdillon et al; a histidine residue or thiol group located in close vicinity of the flavin would be a likely candidate for the binding site [15].…”

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 76%

“…When these data are compared to data of previously investigated mediators, great differences in reactivity are noticed. The rate constants of investigated mediators are close to positively charged oxidized ferrocenes, ferrocene methanol, (dimethylaminomethyl) izrocene, and the promazine dication radical [15]. However, the reactivity of the presently investigated cations are one to two orders of magnitude higher than the reactivity of quinones [8,9,16].…”

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 89%

“…However, the reactivity of the presently investigated cations are one to two orders of magnitude higher than the reactivity of quinones [8,9,16]. The reactivity of TTT is nearly three orders of magnitude higher than that of other ferrocene derivatives in spite of their higher potential [6,15,17,18]. A possible explanation of the high TTT as well as TTF and DMTSF cation reactivities can be accomplished by assuming uncommon self-exchange constants.…”

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 97%

“…quinones, ferricenes etc. [6,8,9,15,16] includes reduction of the enzyme active centre following its oxidation by the cation of mediator: E-FAD + Glucose + E-FADH, + glucono-&lactone…”

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 99%

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Kinetics of glucose oxidase catalyzed electron transfer mediated by sulfur and selenium compounds

Kulys¹,

Buch-Rasmussen

Bechgaard

et al. 1993

FEBS Letters

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Unusually high electron transfer rates in Aspergillus niger glucose oxidase catalyzed oxidation of glucose using 5,6:11,12-Bis(dithio)tetraume (ITT), 1,2-dimethyltetraselenafulvalene (DMTSF) and tetrathiafulvalene (TTF) were observed. At pH 7.0 oxidation rate constants (TN/&,,) in the range from 1.0 . 10' to 8.7 . 10' M . s-' were deduced from experimental data. One of the investigated mediators, DMTSF, has been used for electrocatalytical glucose oxidation on graphite at a potential of 0.3 V vs. a standard calomel electrode (SCE). The prepared bioelectrodes have a sensitivity of 1.3 @/(cm* . mM), a pH optimum at 6.5-7.0, and a linear range which covers the relevant range for monitoring physiological levels of glucose.The bioelectrodes are stable for more than one month.

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Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 76%

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 89%

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 97%

“…quinones, ferricenes etc. [6,8,9,15,16] includes reduction of the enzyme active centre following its oxidation by the cation of mediator: E-FAD + Glucose + E-FADH, + glucono-&lactone…”

Section: The Rate Of Reduced Glucose Oxidase Oxidation In Homogenous mentioning

confidence: 99%

See 2 more Smart Citations

Kinetics of glucose oxidase catalyzed electron transfer mediated by sulfur and selenium compounds

Kulys¹,

Buch-Rasmussen

Bechgaard

et al. 1993

FEBS Letters

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“…Kinetic data obtained by double step chronoamperometry, presented in Table 3, shows that PTZ acts as an efficient mediator for all investigated oxidases. Most previous reports of kinetic studies of mediated bioelectrocatalysis with enzymes are based on electrochemical measurements in homogeneous solutions (Bourdillon et al 1993); (Kulys et al 1994); (Heller and Feldman 2008). Double step chronoamperometry allows the kinetic characteristics of biocatalysts to be estimated even in the immobilised state.…”

Section: Immobilisation Of Different Mediated Oxidasesmentioning

confidence: 99%

Unsubstituted phenothiazine as a superior water-insoluble mediator for oxidases

Sekretaryova

Vagin

Beni

et al. 2014

Biosensors and Bioelectronics

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The mediation of oxidases: glucose oxidase (GOx), lactate oxidase (LOx) and cholesterol oxidase (ChOx) by a new electron shuttling mediator, unsubstituted phenothiazine (PTZ), was studied. Cyclic voltammetry and rotating-disk electrode measurements in nonaqueous media were used to determine the diffusion characteristics of the mediator and the kinetics of its reaction with GOx, giving a second-order rate constant of 7.6 × 10 3 M -1 s -1 to 2.1 × 10 4 M -1 s -1 for water -acetonitrile solutions containing 5 % to 15 % water. These values are in the range reported for commonly used azine-type mediators, indicating that PTZ is able to function as an efficient mediator. PTZ and GOx, LOx and ChOx were successfully co-immobilized in sol-gel membrane on a screen-printed electrode to construct glucose, lactate and cholesterol biosensors, respectively, which were then optimised in terms of stability and sensitivity. The electrocatalytic oxidation responses showed a dependence on substrate concentration ranging from 0.6 to 32 mM for glucose, from 19 to 565 mM for lactate and from 0.015 to 1.0 mM for cholesterol detection.Oxidation of substrates on the surface of electrodes modified with PTZ and enzyme membrane was investigated with double-step chronoamperometry and the results showed that the PTZ 2 displays excellent electrochemical catalytic activities even when immobilised on the surface of the electrode. Highlights: The kinetics of the electrocatalytic oxidation of glucose with GOx mediated by a new electron shuttling mediator, PTZ, was studied. PTZ delivers superior potential performance among azine-type redox mediators for GOx. PTZ and GOx, LOx and ChOx were successfully co-immobilized in sol-gel membrane on a screen-printed electrode to construct glucose, lactate and cholesterol biosensors, respectively. Second-order rate constants for the reaction between the mediator and variety of oxidases co-immobilised inside a sol-gel membrane were obtained by chronoamperometry.

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Construction of multicomponent catalytic films based on avidin-biotin technology for the electroenzymatic oxidation of molecular hydrogen

Lacey

Detcheverry

Moiroux

et al. 2000

Biotechnol. Bioeng.

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A fully active monolayer enzyme electrode derivatized by antigen-antibody attachment

Cited by 213 publications

References 0 publications

Kinetics of glucose oxidase catalyzed electron transfer mediated by sulfur and selenium compounds

Kinetics of glucose oxidase catalyzed electron transfer mediated by sulfur and selenium compounds

Unsubstituted phenothiazine as a superior water-insoluble mediator for oxidases

Construction of multicomponent catalytic films based on avidin-biotin technology for the electroenzymatic oxidation of molecular hydrogen

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