Enzymatic Anodes for Hydrogen Fuel Cells based on Covalent Attachment of Ni‐Fe Hydrogenases and Direct Electron Transfer to SAM‐Modified Gold Electrodes

Rüdiger, Olaf; Gutiérrez-Sánchez, Cristina; Olea, David; Pereira, Inês A. C.; Vélez, Marisela; Fernández, Vı́ctor M.; Lacey, Antonio L. De

doi:10.1002/elan.200880002

Cited by 58 publications

(84 citation statements)

References 39 publications

(45 reference statements)

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“…After 80 h of continuous operation, 25% of the initial current was maintained. A clear DET signal confirmed that the immobilization method favors an orientation where the active site of the enzyme faces the electrode surface [143]. Gutierrez-Sanchez et al reported similar higher operational stability for covalent conjunction of M. verucaria BOD to gold electrodes modified by carboxylate-terminated SAM [145].…”

Section: Effect Of Covalent Attachmentmentioning

confidence: 78%

“…This strategy was applied to various enzymes immobilized on thiol-based SAMs and allowed to determine the surface chemistry on the electrode able to promote DET. One can cite relevant studies that analyzed the catalytic efficiency of A. aeolicus [NiFe]-Hase [142] on negative, positive, or hydrophobic SAMs on gold, of D. gigas Hase on positive SAM on gold [143], of R. eutropha [NiFe]-Hase on negative SAM on silver [61], of Trametes hirsuta LAC on neutral hydrophobic SAM on gold [144], of Cerrena unicolor C139 LAC positive SAM on gold [107], or of Myrothecium verrucaria BOD on positive or negative SAMs on gold [145] (Figure 7). In the latter paper, electrochemistry was coupled to SPR demonstrating that the switching between DET over MET when adsorption was performed either on negative or positive SAM was effectively linked to a different enzyme orientation and not to different enzyme loading.…”

Section: Electrochemistrymentioning

confidence: 99%

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Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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Abstract:Redox enzymes, which catalyze reactions involving electron transfers in living organisms, are very promising components of biotechnological devices, and can be envisioned for sensing applications as well as for energy conversion. In this context, one of the most significant challenges is to achieve efficient direct electron transfer by tunneling between enzymes and conductive surfaces. Based on various examples of bioelectrochemical studies described in the recent literature, this review discusses the issue of enzyme immobilization at planar electrode interfaces. The fundamental importance of controlling enzyme orientation, how to obtain such orientation, and how it can be verified experimentally or by modeling are the three main directions explored. Since redox enzymes are sizable proteins with anisotropic properties, achieving their functional immobilization requires a specific and controlled orientation on the electrode surface. All the factors influenced by this orientation are described, ranging from electronic conductivity to efficiency of substrate supply. The specificities of the enzymatic molecule, surface properties, and dipole moment, which in turn influence the orientation, are introduced. Various ways of ensuring functional immobilization through tuning of both the enzyme and the electrode surface are then described. Finally, the review deals with analytical techniques that have enabled characterization and quantification of successful achievement of the desired orientation. The rich contributions of electrochemistry, spectroscopy (especially infrared spectroscopy), modeling, and microscopy are featured, along with their limitations.

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Section: Effect Of Covalent Attachmentmentioning

confidence: 78%

Section: Electrochemistrymentioning

confidence: 99%

Controlling Redox Enzyme Orientation at Planar Electrodes

et al. 2018

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“…In periplasmic O 2 -sensitive [NiFe]-Hases, an anionic patch of amino acid residues, mainly glutamate residues, surrounds the FeS distal cluster. [88,162] A high dipole moment points towards this cluster. [163] This polarity allows a physiological electrostatic recognition with the positive tetrahemic cytochrome c 3 .…”

Section: Chemelectrochem Reviews Wwwchemelectrochemorgmentioning

confidence: 94%

“…It was demonstrated that H 2 oxidation switches from a direct to a mediated process according to the charge of the SAM. [162,193,194,198] Intriguingly, even with a monolayer of properly oriented Hase, no noncatalytic signals could be observed, precluding a calculation of catalytic turnover (only in the case of a [FeFe]-Hase did the coupling between electrochemistry on SAM electrodes and electrochemical scanning tunneling microscopy allow a turnover frequency of 21,000 s À1 for hydrogen production to be calculated). [199] No explanation can as yet be given for such a result.…”

Section: Hydrogenasesmentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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Among sustainable alternatives to fossil fuel, proton exchange membrane fuel cells are promising devices that deliver electricity from hydrogen and oxygen, producing only water. The transformation of the fuel and oxidant however relies on rare‐metal catalysts. H2/O2 enzymatic biofuel cells thus emerge as sustainable biotechnological devices in which chemical catalysts are replaced by hydrogenases at the anode and multicopper oxidases at the cathode. This review discusses the recent breakthroughs and the limitations in all the components of H2/O2 biofuel cells: 1) Catalytic mechanisms involved in multicopper oxidases and hydrogenases, in addition to the new potential of enzymes from the biodiversity pool, which exhibit outstanding properties. 2) The molecular basis for oriented enzyme immobilization on the electrochemical interfaces as a prerequisite for a fast direct electron‐transfer rate. 3) The requirement for 3D networks to enhance current densities. 4) The production of H2 from biomass. 5) The history of H2/O2 biofuel cells and recent devices, which also highlights the remaining issues that will allow the use of such devices in low‐power applications.

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“…þ to H 2 and the oxidation of H 2 to 2H þ , and their electrochemistry has been explored for over 30 years [63][64][65][66].…”

Section: Direct Bioelectrocatalysis Of Metalloenzymesmentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

166

148

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Enzymatic bioelectrocatalysis is being increasingly exploited to better understand oxidoreductase enzymes, to develop minimalistic yet specific biosensor platforms, and to develop alternative energy conversion devices and bioelectrosynthetic devices for the production of energy and/or important chemical commodities. In some cases, these enzymes are able to electronically communicate with an appropriately designed electrode surface without the requirement of an electron mediator to shuttle electrons between the enzyme and electrode. This phenomenon has been termed direct electron transfer or direct bioelectrocatalysis. While many thorough studies have extensively investigated this fascinating feat, it is sometimes difficult to differentiate desirable enzymatic bioelectrocatalysis from electrocatalysis deriving from inactivated enzyme that may have also released its catalytic cofactor. This article will review direct bioelectrocatalysis of several oxidoreductases, with an emphasis on experiments that provide support for direct bioelectrocatalysis versus denatured enzyme or dissociated cofactor. Finally, this review will conclude with a series of proposed control experiments that could be adopted to discern successful direct electronic communication of an enzyme from its denatured counterpart.

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Enzymatic Anodes for Hydrogen Fuel Cells based on Covalent Attachment of Ni‐Fe Hydrogenases and Direct Electron Transfer to SAM‐Modified Gold Electrodes

Cited by 58 publications

References 39 publications

Controlling Redox Enzyme Orientation at Planar Electrodes

Controlling Redox Enzyme Orientation at Planar Electrodes

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

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Enzymatic Anodes for Hydrogen Fuel Cells based on Covalent Attachment of Ni‐Fe Hydrogenases and Direct Electron Transfer to SAM‐Modified Gold Electrodes

Cited by 58 publications

References 39 publications

Controlling Redox Enzyme Orientation at Planar Electrodes

Controlling Redox Enzyme Orientation at Planar Electrodes

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Contact Info

Product

Resources

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Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective