Oriented Immobilization of Desulfovibrio gigas Hydrogenase onto Carbon Electrodes by Covalent Bonds for Nonmediated Oxidation of H2

Rüdiger, Olaf; Abad, José M.; Hatchikian, E.C.; Fernández, Vı́ctor M.; Lacey, Antonio L. De

doi:10.1021/ja0554312

Cited by 151 publications

(171 citation statements)

References 23 publications

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“…MBH was chemically immobilized on the KBGCE through the amidelinkage 32,33 to avoid the desorption of MBH under strongly convective conditions. The bare KBGCE was electrochemically pretreated to generate 4-aminophenyl layer on the surface according to the literature with minor modification.…”

Section: Methodsmentioning

confidence: 99%

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

Kitazumi

Shirai

et al. 2014

Bulletin of the Chemical Society of Japan

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Membrane-bound [NiFe]-hydrogenase (MBH) from Hydrogenovibrio marinus is an O 2 -tolerant enzyme and allows direct-electron-transfer (DET) bioelectrocatalysis for H 2 -oxidation. MBH is a promising bioelectrocatalyst for bioanode of enzymatic H 2 O 2 biofuel cells. From the practical viewpoint of electricity production, the H 2 -depletion near the electrode surface and the oxidative and reversible inactivation called "anaerobic inactivation" of [NiFe]-hydrogenases limit the H 2 -oxidation at high potentials. We have already proposed a gas-diffusion system to avoid inactivation in our previous study. In this research, we have analyzed the kinetics of the electrochemically induced anaerobic inactivation and the DET bioelectrocatalytic reaction of MBH on electrodes. When the inactivation is considered as a competitive inhibition-like reaction, the maximum value of the apparent Michaelis constant reaches 6.5 mM (at Ketjen Black-modified electrode) as analyzed in our kinetic model. Since the value is larger than the saturated H 2 -concentration in solution (0.74 mM), we conclude that high-speed H 2 -supply realized by a gas-diffusion electrode is essential to compete with the inactivation. Furthermore, a gas-diffusion bioanode with MBH can eliminate the H 2 -depletion near the electrode surface and has reached about 10 mA cm ¹2 at 0 V (vs. Ag«AgCl«sat. KCl electrode) under quiescent (passive) and H 2 -atmospheric conditions.Hydrogenases are enzymes which catalyze the interconversion between hydrogen and proton.1 The two major classes of hydrogenases are known as [FeFe] or [NiFe] according to the metals in their buried active sites.1,2 Since hydrogenases are highly active, with turnover frequencies for H 2 -oxidation in excess of thousands of molecules of H 2 per second at 30°C, 3 they can be alternative catalysts instead of platinum as an H 2 O 2 fuel cell.4 From the aspect of bioelectrochemistry, hydrogenases have received a lot of attention, and the bioelectrocatalytic properties have extensively been characterized all over the world. 1,2,58 Enzymatic biofuel cells, which are electric generators that utilize redox enzymes as catalysts, can generally operate under mild conditions (neutral pH, atmospheric pressure, and room temperature). They are classified into two types: mediated electron transfer (MET)-type and direct electron transfer (DET)-type.912 MET-type cell utilizes artificial mediators to shuttle the electron between the enzyme and the electrode to reduce the kinetic hindrance in the interfacial electron transfer. On the other hand, DET-type cell does not require, in principle, any separator or membrane between the electrodes due to the mediator-less configuration. In addition, the DET-type one can reduce the possible health hazard problems caused by artificial mediators and the thermodynamic loss ascribed to the difference in the redox potentials between the mediator and the active site of the enzyme. Furthermore, the DET-type system enables us to construct a very simple and compact enzymatic biofuel ...

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Section: Methodsmentioning

confidence: 99%

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

Kitazumi

Shirai

et al. 2014

Bulletin of the Chemical Society of Japan

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“…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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“…13 Many strategies have been reported for immobilizing hydrogenases on electrodes, such as physical adsorption, [14][15][16][17][18] covalent bonding 19,20 , entrapment in redox polymers 21,22 and layer-by-layer deposition 23,24 . Charge exchange between the electrode and the hydrogenase has been achieved in some strategies by DET, [14][15][16][17][18]20 whereas in others by mediated electron transfer (MET). 19,[21][22][23][24] In previous works we have developed a robust and controlled immobilization method of the soluble hydrogenase from Desulfovibrio gigas onto different types of electrodes, based on electrostatic interactions directing the correct orientation of the enzyme for DET.…”

Section: Introductionmentioning

confidence: 99%

Oriented Immobilization of a Membrane-Bound Hydrogenase onto an Electrode for Direct Electron Transfer

et al. 2011

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The ACS journal of surfaces and colloids 27: 6449-6457 (2011) 2 ABSTRACTThe interaction of redox enzymes with electrodes is of great interest for studying the catalytic mechanisms of redox enzymes and for bioelectronic applications. Efficient electron transport between the biocatalysts and the electrodes has achieved more success with soluble than with membrane enzymes due to the higher structural complexity and instability of the latter proteins. In this work we report a strategy for immobilizing a membrane-bound enzyme onto gold electrodes with a controlled orientation in its fully active conformation. The immobilized redox enzyme is the Ni-Fe-Se hydrogenase from Desulfovibrio vulgaris Hildenborough, which catalyzes H 2 -oxidation reversibly and is associated to the cytoplasmic membrane by a lipidic tail. Gold surfaces modified with this enzyme and phospholipids have been studied by atomic force microscopy (AFM) and electrochemical methods. The combined study indicates that by a two-step immobilization procedure the hydrogenase can be inserted via its lipidic tail onto a phospholipidic bilayer formed over the gold surface, only allowing mediated electron transfer between enzyme and electrode. On the other hand, a one-step immobilization procedure favours formation of a hydrogenase monolayer over the gold surface with its lipidic tail inserted in a phospholipid bilayer formed on top of the hydrogenase molecules. This latter method has allowed for the first time efficient electron transfer between a membrane-bound enzyme in its native conformation and an electrode.

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Oriented Immobilization of Desulfovibrio gigas Hydrogenase onto Carbon Electrodes by Covalent Bonds for Nonmediated Oxidation of H₂

Cited by 151 publications

References 23 publications

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

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

Oriented Immobilization of a Membrane-Bound Hydrogenase onto an Electrode for Direct Electron Transfer

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Oriented Immobilization of Desulfovibrio gigas Hydrogenase onto Carbon Electrodes by Covalent Bonds for Nonmediated Oxidation of H2

Cited by 151 publications

References 23 publications

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

Kinetic Analysis of Inactivation and Enzyme Reaction of Oxygen-Tolerant [NiFe]-Hydrogenase at Direct Electron-Transfer Bioanode

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

Oriented Immobilization of a Membrane-Bound Hydrogenase onto an Electrode for Direct Electron Transfer

Contact Info

Product

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Oriented Immobilization of Desulfovibrio gigas Hydrogenase onto Carbon Electrodes by Covalent Bonds for Nonmediated Oxidation of H₂

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