Wiring of pyranose dehydrogenase with osmium polymers of different redox potentials

Zafar, Muhammad Nadeem; Tasca, Federico; Boland, Susan; Kujawa, Magdalena; Patel, Ilabahen; Peterbauer, Clemens K.; Leech, Dónal; Gorton, Lo

doi:10.1016/j.bioelechem.2010.04.002

Cited by 62 publications

(59 citation statements)

References 29 publications

(62 reference statements)

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“…1S, SI), avoiding the diffusion of the mediator out of the enzyme film at the electrode surface, has been used. This wiring approach was previously used to achieve bioelectrocatalysis of such FAD containing enzymes as glucose oxidase (Gregg and Heller, 1990;Mao et al, 2003), diaphorase (Antiochia and Gorton, 2007;Tasca et al, 2008;Tsujimura et al, 2002a), pyranose oxidase (Timur et al, 2006;Zafar et al, 2010), FAD-dependent glucose dehydrogenase (Zafar et al, 2012) and in the development of O 2 -reducing biocathodes based on blue-copper enzymes such as laccases (Barriere et al, 2004;Daigle et al, 1998) and bilirubin oxidase (Mano et al, 2002;Tsujimura et al, 2002b). It was also successfully used for wiring of the redox centers of such a fragile membrane enzyme complex as theophylline oxidase (Shipovskov and Ferapontova, 2008), providing retention of its bioelectrocatalytic activity within the polymer matrix (Ferapontova et al , 2006), and even those of whole cells (Coman et al, 2009;Hasan et al, 2012;Vostiar et al, 2004).…”

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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“…However, when in a previous investigation (55), 6 different Os-polymers with E°'-value ranging between +15 and +489 mV vs. NHE, it was shown that Os-polymer [Os(dmbpy) 2 (PVI) 10 Cl] + very efficiently could "wire" GcGDH. That Os-polymer is also an efficient "wire" for AmPDH was also shown in (21). Therefore for co-immobilized AmPDH/GcGDH, that Os-polymer was used and the structure of Os polymer is shown in figure 1.…”

Section: Resultsmentioning

confidence: 97%

“…From previous spectroelectrochemical and "wiring" investigations of AmPDH (13,21), the E°'-value of the bound FAD in AmPDH was determined to be +150 mV vs. NHE. The E°'-value of the bound FAD in GcGDH is not known.…”

Section: Resultsmentioning

confidence: 99%

Improving the Current Density and the Coulombic Efficiency by a Cascade Reaction of Glucose Oxidizing Enzymes

Zafar

Shao

Ludwig³

et al. 2013

ECS Trans.

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Improvements in current density and coulombic efficiency of a glucose oxidizing electrode were realized by a combination of pyranose dehydrogenase from Agaricus meleagris (AmPDH) with glucose dehydrogenase from Glomerella cingulata (GcGDH). The mixed enzyme electrode oxidizes glucose in several combinations at the C-1, C-2 and C-3 positions of the pyranose ring. This concerted action of enzymes increases (i) the coulombic efficiency by extracting more than 2e -per substrate molecule and (ii) the current density of the electrode when the mass-transfer of substrates becomes rate limiting. The electrodes were investigated with flow injection analysis (FIA) using different substrates under physiological conditions (pH 7.4). These investigations showed that the product of one enzyme can be used as substrate for the other enzyme and maximally 6e -can be gained from the oxidation of one glucose molecule using mixed enzyme electrode AmPDH/GcGDH/Ospolymer. We propose a bioanode for use in biofuel cells with an increased current density and coulombic efficiency obtained by a cascade reaction catalyzed by redox enzymes with a different site-specificity for glucose. 10.1149/05302.0131ecst ©The Electrochemical Society ECS Transactions, 53 (2) 131-143 (2013) 131 ) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 128.210.126.199 Downloaded on 2015-07-06 to IP

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“…The Gorton research group has been pioneers in alternative glucose oxidizing enzymes [39][40][41][42][43][44] and has been evaluating and utilizing these alternative enzymes for sugar oxidation cascades. Gorton et al developed an artificial 2 enzyme cascade for deep oxidation of sugars utilizing promiscuous enzymes [45].…”

Section: Minimal and Artificial Enzyme Cascadesmentioning

confidence: 99%

Oxidative bioelectrocatalysis: From natural metabolic pathways to synthetic metabolons and minimal enzyme cascades

Minteer

2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Anodic bioelectrodes for biofuel cells are more complex than cathodic bioelectrodes for biofuel cells, because laccase and bilirubin oxidase can individually catalyze four electron reduction of oxygen to water, whereas most anodic enzymes only do a single two electron oxidation of a complex fuel (i.e. glucose oxidase oxidizing glucose to gluconolactone while generating 2 electrons of the total 24 electrons), so enzyme cascades are typically needed for complete oxidation of the fuel. This review article will discuss the lessons learned from natural metabolic pathways about multi-step oxidation and how those lessons have been applied to minimal or artificial enzyme cascades. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.

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Wiring of pyranose dehydrogenase with osmium polymers of different redox potentials

Cited by 62 publications

References 29 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

Improving the Current Density and the Coulombic Efficiency by a Cascade Reaction of Glucose Oxidizing Enzymes

Oxidative bioelectrocatalysis: From natural metabolic pathways to synthetic metabolons and minimal enzyme cascades

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