Miniature direct electron transfer based sulphite/oxygen enzymatic fuel cells

Zeng, Ting; Pankratov, Dmitry; Falk, Magnus; Leimkühler, Silke; Shleev, Sergey; Wollenberger, Ulla

doi:10.1016/j.bios.2014.10.080

Cited by 23 publications

(35 citation statements)

References 30 publications

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“…Direct electrochemistry using different electrode materials was observed for sulfite dehydrogenase, and sulfite oxidase . A DET based sulfite/oxygen biofuel cell was reported using human sulfite oxidase and bilirubin oxidase on modified gold electrodes . Power densities of 1 and 8 μW cm −2 were achieved at different polarization potentials.…”

Section: Multi‐cofactor Oxidoreductases Carrying a Cytochromementioning

confidence: 99%

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Ludwig

2018

ChemElectroChem

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The direct electron transfer (DET) of enzymes has been utilized to develop biosensors and enzymatic biofuel cells on micro‐ and nanostructured electrodes. Whereas some enzymes exhibit direct electron transfer between their active‐site cofactor and an electrode, other oxidoreductases depend on acquired cytochrome domains or cytochrome subunits as built‐in redox mediators. The physiological function of these cytochromes is to transfer electrons between the active‐site cofactor and a redox partner protein. The exchange of the natural electron acceptor/donor by an electrode has been demonstrated for several cytochrome carrying oxidoreductases. These multi‐cofactor enzymes have been applied in third generation biosensors to detect glucose, lactate, and other analytes. This review investigates and classifies oxidoreductases with a cytochrome domain, enzyme complexes with a cytochrome subunit, and covers designed cytochrome fusion enzymes. The structurally and electrochemically best characterized proponents from each enzyme class carrying a cytochrome, that is, flavoenzymes, quinoenzymes, molybdenum‐cofactor enzymes, iron‐sulfur cluster enzymes, and multi‐haem enzymes, are featured, and their biochemical, kinetic, and electrochemical properties are compared. The cytochromes molecular and functional properties as well as their contribution to the interdomain electron transfer (IET, between active‐site and cytochrome) and DET (between cytochrome and electrode) with regard to the achieved current density is discussed. Protein design strategies for cytochrome‐fused enzymes are reviewed and the limiting factors as well as strategies to overcome them are outlined.

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Section: Multi‐cofactor Oxidoreductases Carrying a Cytochromementioning

confidence: 99%

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Ludwig

2018

ChemElectroChem

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“…Sulfite oxidase and the closely related bacterial sulfite dehydrogenases have been immobilized on pyrolytic graphite edge electrodes 19,20 , gold electrodes modified with thiols 21 or nanoparticles [22][23][24] , and silver electrodes 25 , either to gain mechanistic information, or in the perspective of constructing sulfite biosensors 26 or the anodes of sulfite-based biofuel cells 27 .…”

Section: Introductionmentioning

confidence: 99%

Transient Catalytic Voltammetry of Sulfite Oxidase Reveals Rate Limiting Conformational Changes

et al. 2017

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Sulfite oxidases are metalloenzymes that oxidize sulfite to sulfate at a molybdenum active site. In vertebrate sulfite oxidases, the electrons generated at the Mo center are transferred to an external electron acceptor via a heme domain, which can adopt two conformations: a "closed" conformation, suitable for internal electron transfer, and an "open" conformation suitable for intermolecular electron transfer. This conformational change is an integral part of the catalytic cycle. Sulfite oxidases have been wired to electrode surfaces, but their immobilization leads to a significant decrease in their catalytic activity, raising the question of the occurrence of the conformational change when the enzyme is on an electrode. We recorded and quantitatively modeled for the first time the transient response of the catalytic cycle of human sulfite oxidase immobilized on an electrode. We show that conformational changes still occur on the electrode, but at a lower rate than in solution, which is the reason for the decrease in activity of sulfite oxidases upon immobilization.

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“…Bioelectrocatalysis is an attractive way to employ redox enzymes in technical devices, such as miniaturized sensors, fuel cells and for synthesis of otherwise difficult to produce compounds . The direct electronic coupling between the active site and the electrode should allow electron transfer at no (or low) overpotential and thus minimum loss of driving force and without parasitic reactions.…”

Section: Introductionmentioning

confidence: 99%

Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase

et al. 2016

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1Introduction Molybdenum (Mo) containing enzymes have been associated with the catalysis of important reactions in the metabolism of smallm oleculess uch as carbon nitrogen, and sulfur [1a, b].T he sulfite oxidizing enzymes sulfite oxidase (SO) and sulfite dehydrogenase (SDH) catalyze the oxidation of sulfite to sulfate accompaniedw ith the release of two electrons and two protons according to the following equation:All sulfite oxidizing enzymes share the same catalytic Mo cofactor (Moco) containingu nit. But the number and type of additional redoxc enters differb etween enzymes from different classes of organisms, which has an impact on the type of electrona cceptor the enzyme can use [2a, b].O nly in the vertebrate SO ah eme b binding domaini sc ovalently linkedt ot he core structure of the enzyme.T he human sulfite oxidase (hSO) shows al arge structural homology to the enzyme from chicken liver (cSO) which is ad imeric enzyme where each subunit of the homodimer consists of an N-terminal heme b binding domain( SO-HD), followed by ap olypeptide tetherc onnectingt he heme domain to the Moco-containing domain (SO-MD) and ad imerization domain at the C-terminus [3].Thes ingle steps of the SO catalyzed reaction involve the two-electron oxidationo fs ulfite to sulfate at the Moco center, where Mo VI is reduced to Mo IV .I nv ertebrate SO the Mo VI regeneration is naturally coupled to the reduction of two equivalents of soluble cytochrome c which proceeds in two subsequent intra-and intermolecular singlee lectron transfer steps via the heme b5 containing site [4a, b, c].T hese steps involve ar epositioning of the domains to reduce electron transfer distances permitting electron transfer from Mo to Fe of SO-HD and to cytochrome c [5a, b].Areaction with soluble [6a, b] and polymerb ound redoxm ediators is also possible [7a, b]. Direct unmediated electron transfer from the reduced enzyme to electrodes proceedsv ia the hemed omain [8]. This process was most effective when the enzymei si mmobilized on electrode surfaces modified with positive charged SAMs facilitating the oriented assembly of SO electron transfer and bioelectrocatalysis [9a, b].Abstract:W er eport efficient bioelectrocatalytic sulfite oxidation by human sulfite oxidase (hSO) immobilizedo n ag old nanoparticle (AuNP)m odified gold electrode.T he AuNP were synthesized in aqueous phase by using branched polyethyleneimine (PEI) as reducing as well as stabilizing agent. Golde lectrodes were modified by as elf assembled monolayer of dithio-bis(N-hydroxysuccinimidyl propionate) (DTSP) onto which the NP and hSO were immobilized. Cyclic voltammetry of the hSO modified electrode in the absence of substrater evealedaquasi-reversible direct electrochemical reactiono ft he heme domaino fhSO with fast electron transfer rate.T he electron transferr ate constant of k s = 32 s À1 and the formal potential E 0 ' = À0.155 Vv s. Ag/AgCl/1 MK Cl were estimated. Comparatives tudies with nanoparticles of BaSO 4 indicate the importance of the NP conductivity for charge transfer an...

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Miniature direct electron transfer based sulphite/oxygen enzymatic fuel cells

Cited by 23 publications

References 30 publications

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Direct Electron Transfer of Enzymes Facilitated by Cytochromes

Transient Catalytic Voltammetry of Sulfite Oxidase Reveals Rate Limiting Conformational Changes

Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase

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