Oxidation bioelectrocatalyzed

Figure 1.30 Magneto-switched bioelectrocatalyzed oxidation of glucose in the presence of relay-functionalized magnetic particles. (Reprinted with permission from Ref [157]. 2000 American Chemical Society.)...

Scheme 10.3 Amplified detection of Viral DNA by the generation of a redox-active replica and the bioelectrocatalyzed oxidation of glucose. Reprinted with permission from Ref. 94. Copyright 2002 American Chemical Society.

Cyclic voltammograms of the COx/Cyt.c electrode corresponding to the bioelectrocatalyzed reduction of 02 (i), and to the reference system, where 02 is excluded (ii). (c) Assembly of an integrated LDH electrode for the bioelectrocatalyzed oxidation of lactate by the surface cross-linking of an affinity complex formed between LDH and different structures of a boronate-linked PQQ-NAD monolayer. Parts (a) and (b) Reproduced from Ref. 27 by permission of the Royal Society of Chemistry (RSC). Part (c) Reproduced with permission from Ref. 25. Copyright 2002 American Chemical Society. 

Fig. 9 Photostimulated bioelectrocatalyzed oxidation of glucose (2.5 x 10-2 M) in the presence of ferrocenecarboxylic acid (23)...

GOx (22a). (b) protonated nitromerocyanine-tethered GOx, (22b). I nset Reversible photo-switchable amperometric transduction of the bioelectrocatalyzed oxidation of glucose by 22a - ( ) and 22b-(o). 

Fig. 12 Photoswitchable bioelectrocatalyzed oxidation of glucose (8 x 10-2 M) by a composite monolayer consisting of COx reconstituted onto FAD units and nitrospiropyran photoi-somerizable units in the presence of 29 as a diffusional electron mediator, (a) In the presence...

Figure 12.4 Photoinduced bioelectrocatalyzed oxidation of glucose to gluconic acid by glucose oxidase (COD) reconstituted with a nitrospiropyran-modified FAD cofactor (Sp-FAD) assembled as a monolayer on the Au electrode. Fhe Sp-FAD reveals reversible photoisomeriz-able properties yielding nitromerocyanine-FAD isomer (MRH+-FAD) [34]...

Raitman OA, Katz E, Biickmann AF et al (2002) Integration of polyaniline/poly(acrylic acid) films and redox enzymes on electrode supports an in situ electrochemical/surface plasmon resonance study of the bioelectrocatalyzed oxidation of glucose or lactate in the integrated bioelectrocatalytic systems. J Am Chem Soc 124 6487-6496... 

Fig. 5 Immobilized nucleic acid assays utilizing redox-active moieties, a Amplified detection of viral DNA by generation of a redox-active replica and the bioelectrocatalyzed oxidation of glucose (Reprinted with permission from [200]. Copyright(2002) American Chemical Society), b Alternative formats for the capture on a gold electrode SAM of solution-extended primers or direct surface extension of primer with electrotides (adapted from [185]). c Ferrocene-labelled hairpin for electrochemical DNA hybridization detection. A Fc-hairpin-SH macromolecule is immobilized on a gold electrode. When a complementary DNA target strand binds to the hairpin, it opens and the ferrocene redox probe is separated from the electrode, producing a decrease in the observed current (Reprinted with permission from [203], Copyright(2004) American Chemical Society)...

Figure 3. The enantioselective bioelectrocatalyzed oxidation of glucose by glucose oxidase at an electrode modified by a chiral electron-transfer mediator. (A) Organization of the chiral ferrocene monolayer-modified Au electrode and its interaction with soluble GOx. EDC = l-(3-dimethylami-nopropyl)-3-ethylcarbodiimide hydrochloride. (B) Cyclic voltammograms of the ferrocene-modified electrode (curves a and b for (i )-Fc (2) and (5)-Fc (3), respectively) in the presence of 1 x 10 M GOx and 50 mM glucose 0.1 M phosphate buffer, pH 7.0 potential scan rate, 5 mV s electrode area, 0.26 cm. ...

Figure 8. (A) The assembly of an electrically contacted glutathione reductase monolayer. (B) The rate of bioelectrocatalyzed reduction of oxidized glutathione (GSSG) by the electrically contacted enzyme electrode using various connecting chain lengths (a) n = 2, (b) n = 5, (c) = 11. Application of -0.72 V vs. SCE to the enzyme electrode in the presence of GSSG (10 mM). The experiments were performed in 0.1 M phosphate buffer, pH 7.2, under Ar.

Figure 3-5. (A) Assembly of reconstituted glucose oxidase on a PQQ-FAD monolayer linked to an Au-electrode. (H i Faradaic impedance spectra of the modified electrode at time intervals of reconstitution, (a) 0.1 h, (b) 0.25 h. (c) 0.5 h. (d) 1 h. (e) 2 h, (f) 4 h. Inset Interfacial electron transfer resistance of the modified electrode at time-intervals of reconstitution. (C) Cyclic voltammograms corresponding to the bioelectrocatalyzed oxidation of glucose, 80 mM, by the enzyme-functionalized electrode at time-intervals of reconstitution (a) 0 h, (b) 0.1 h, (c) 0.25 h, (d) 0.5 h, (e) 1 h, (f) 2 h, (g) 4 h. Inset Electrocatalytic currents transduced by the enzyme-modified electrode at time-intervals of reconstitution. Reproduced with permission from ref. 32. Copyright 2002 American Chemical Society.

Figure 3-8. Cyclic voltammograms corresponding to the bioelectrocatalyzed oxidation of variable concentrations of glucose by the integrated, electrically-contacted polyaniline-reconstituted glucose oxidase electrode. Glucose concentrations correspond to (a) 0 mM, (b) 5 rnM. (c) 10 mM, (d) 20 mM, (e) 35 inM. (1) 50 mM. Reproduced with permission from ref. 34. Copyright 2002 American Chemical Society.

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