Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors

Gorton, Lo; Lindgren, Annika; Larsson, T.; Munteanu, Florentina; Ruzgas, Tautgirdas; Gazaryan, I. G.

doi:10.1016/s0003-2670(99)00610-8

Cited by 520 publications

(296 citation statements)

References 110 publications

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“…Nowadays, this charge transfer process is a central issue in the development of nanobiotechnological devices, such as biosensors for health monitoring or enzymatic fuel cells [3][4][5][6] .…”

Section: Introductionmentioning

confidence: 99%

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

et al. 2017

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The direct electron transfer (DET) to redox proteins has become a central topic in the development of biotechnological devices. The present work explores the mechanisms of the direct electrochemistry between cytochrome c and a conducting polymer, PEDOT-PSS. This polymer has been electrosynthesized from its monomers in aqueous solution on gold electrodes and its capabilities for DET to cyt c have been examined by electrochemical and spectroelectrochemical methods. The polymer was electrodeposited with controlled thickness and we determined the electron transfer rate constant for cyt c oxidation was about 2 orders of magnitude higher than those obtained at conventional electrodes. Spectroelectrochemical measurements allowed to evaluate the redox state of the polymer as a function of the potential and, in addition, the observation of intrinsic cyt c redox activity upon electron transfer from the conducting polymer. During the oxidation process of this protein, lysine residues placed near the heme crevice interact electrostatically with the anionic polyelectrolyte PSS. This interaction favors the orientation of the heme group towards the chains of PEDOT backbone, which is the eventual responsible for the electron transfer to the protein.3

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Section: Introductionmentioning

confidence: 99%

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

et al. 2017

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“…When the effect of the applied potential was investigated, an independence of the intensity of the steady state current for theophylline and the applied potential was registered for potentials between -0.1 and +0.2 V vs. AgAgCl. The E°' of the cytochrome domain of many of the heme containing redox enzymes at pH 7 is found below 0 V AgAgCl (Gorton et al, 1999;Schuhmann et al 2000;Lindgren et al, 2000;Aguey-Zinsou et al, 2003;Ferapontova, 2003). The E°'-value of the heme in ThO is not to be found in the literature but should be lower than that of cyt.…”

Section: Tho-modified Graphite Electrodesmentioning

confidence: 84%

“…In many of the previous initial claims for DET communication between a redox enzyme and an electrode only indirect proofs prevail, i.e., only in the presence of the enzyme substrate indications of direct electron transfer can be seen (Gorton et al, 1999). However, when exchanging graphite for, e.g., thiol modified gold, independent electrochemical proofs, i.e., in the absence of enzyme substrate, true mediatorless electron transfer has been shown for, e.g., cellobiose dehydrogenase , alcohol PQQ dehydrogenase (Schuhmann, et al, 2000), sulphite oxidase (Ferapontova et al, 2003) characteristics between the redox enzyme and the electrode (Larsson, et al, 2001).…”

Section: Spectrelectrochemistry Of Tho On Aldrithiol Modified Gold Elmentioning

confidence: 99%

“…In several additional cases researchers have proved that the natural electron acceptor/donor can be replaced by an electrode surface for some other redox enzymes, showing that a direct electronic communication can also occur between a redox enzyme and an electrode (Tarasevich, et al, 1979, Ghindilis, et al, 1997, Armstrong and Wilson, 2000. For heme containing redox enzymes, direct electron transfer (DET) between the heme group and the electrode has been postulated and in many cases demonstrated (Gorton, et al, 1999). The two properties of ThO, (i) its fast redox reaction with cyt.…”

Section: Introductionmentioning

confidence: 99%

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Direct heterogeneous electron transfer of theophylline oxidase

Christenson

Dock

Gorton

et al. 2004

Biosensors and Bioelectronics

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“…In this work LPO adsorption was studied on gold substrates which due to the electrical conductivity provide possibilities to measure the activity of surface bound LPO by electrochemical means, as illustrated by Fig. 1 (described in Section 3.3), based on our earlier electrochemical studies of peroxidases [16,17].…”

Section: Adsorption Of Lactoperoxidase On Bare Gold Surfacesmentioning

confidence: 99%

Activity of lactoperoxidase when adsorbed on protein layers

Haberska

Svensson

Shleev

et al. 2008

Talanta

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. Contents lists available at ScienceDirect Talanta j o u r n a l h o m e p a g e : w w w . e l s e v i e r . c o m / l o c a t e / t a l a n t a b s t r a c tLactoperoxidase (LPO) is an enzyme, which is used as an antimicrobial agent in a number of applications, e.g., food technology. In the majority of applications LPO is added to a homogeneous product phase or immobilised on product surface. In the latter case, however, the measurements of LPO activity are seldom reported. In this paper we have assessed LPO enzymatic activity on bare and protein modified gold surfaces by means of electrochemistry. It was found that LPO rapidly adsorbs to bare gold surfaces resulting in an amount of LPO adsorbed of 2.9 mg/m 2 . A lower amount of adsorbed LPO is obtained if the gold surface is exposed to bovine serum albumin, bovine or human mucin prior to LPO adsorption. The enzymatic activity of the adsorbed enzyme is in general preserved at the experimental conditions and varies only moderately when comparing bare gold and gold surface pretreated with the selected proteins. The measurement of LPO specific activity, however, indicate that it is about 1.5 times higher if LPO is adsorbed on gold surfaces containing a small amount of preadsorbed mucin in comparison to the LPO directly adsorbed on bare gold.

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Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors

Cited by 520 publications

References 110 publications

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

Direct Electron Transfer to Cytochrome c Induced by a Conducting Polymer

Direct heterogeneous electron transfer of theophylline oxidase

Activity of lactoperoxidase when adsorbed on protein layers

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