A H 2 /O 2 enzymatic fuel cell as a sustainable power for a wireless device

Monsalve, Karen; Mazurenko, Ievgen; Lalaoui, Noémie; Goff, Alan Le; Holzinger, Michael; Infossi, Pascale; Nitsche, S.; Lojou, Jean-Yves; Giudici‐Orticoni, Marie‐Thérèse; Cosnier, Serge; Lojou, Élisabeth

doi:10.1016/j.elecom.2015.09.014

Cited by 35 publications

(36 citation statements)

References 26 publications

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“…The Aa MbH is a thermostable enzyme showing the highest H 2 oxidation activity at a temperature of 85 °C. It can, however, oxidize H 2 over a wide temperature range if immobilized either on oxidized CNTs or on carbon nanofibers . Enzymes often show improved stability upon immobilization on a solid support .…”

Section: Resultsmentioning

confidence: 99%

“…Comprehensive electrochemical studies based on enzyme adsorption on graphite electrodes have allowed the crucial catalytic parameters of the enzymes to be determined . The Aa MbH has, furthermore, been used as the bioanode catalyst in H 2 /O 2 EFCs that were shown to deliver sufficient power to run a wireless electronic device …”

Section: Introductionmentioning

confidence: 99%

“…This can be achieved by using three‐dimensional networks with high surface/volume ratios . Gold nanoparticles, carbon nanotubes (CNTs), carbon nanofibers, and carbon felt post‐functionalized by CNTs were shown to efficiently adsorb the Aa MbH . Various carbon nanoparticles were also compared in terms of their capabilities to catalyze H 2 oxidation by immobilization of another O 2 ‐tolerant hydrogenase ( E. coli Hyd‐1) .…”

Section: Introductionmentioning

confidence: 99%

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Impact of Carbon Nanotube Surface Chemistry on Hydrogen Oxidation by Membrane‐Bound Oxygen‐Tolerant Hydrogenases

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Impact of Carbon Nanotube Surface Chemistry on Hydrogen Oxidation by Membrane‐Bound Oxygen‐Tolerant Hydrogenases

et al. 2016

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“…[49] Furthermore, state-of-the-art strategies eliminate noble metals altogether by the use of alternative low cost materials based on transition metals such as Fe or Co, [50][51][52][53] material morphologies with a highly catalytic active surface, [54] or hydrogenase-based enzymatic catalysts. [55] It is expected that these strategies will provide effective solutions to reduce the electrode cost.…”

Section: Integration Of Hydrogen Fuel Cell Stripmentioning

confidence: 99%

Single-use paper-based hydrogen fuel cells for point-of-care diagnostic applications

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Lim

et al. 2017

Journal of Power Sources

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This work demonstrates a stand-alone power source that integrates a paper-based hydrogen fuel cell with a customized chemical heater that produces hydrogen in-situ upon the addition of a liquid. The presented approach operates by capillary action and takes advantage of the hydrogen released as a by-product of an exothermic reaction used in point-of-care diagnostics. The paperbased fuel cell produces a maximum power of 25.8 mW (103.2 mW cm -2 ), which is suitable for powering a diversity of electrical devices such as commercially available digital pregnancy tests and glucometers. While device shape and dimensions can be customized, here it is shown that the fuel cell can be designed in a compact form factor and footprint comparable to a lateral flow test while providing a remarkable power output. This approach holds great promise for powering portable diagnostics, as the generated electric power could enable device functionalities required for advanced assays, such as device timing, actuation, and signal quantification. Part of the same liquid sample that is to be analyzed (urine, saliva, water, etc) could be used to trigger the hydrogen generation and start the fuel cell operation.

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“…[12] Thedesign of these nanowires is based on the self-assembly of ap rion domain into amyloid fibers,w ith ad iameter of 3nm and an aspect ratio of 4000. [15][16][17][18] Depending on the required conditions, anaerobic inactivation at high potentials is however an issue. Genes coding for the prion domain of HET-s (from Podospora anserina) and for rubredoxin (Rd) from Methanococcus voltae were fused and cloned in E. coli to express the chimeric protein Rd-HET.…”

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confidence: 99%

Interprotein Electron Transfer between FeS‐Protein Nanowires and Oxygen‐Tolerant NiFe Hydrogenase

et al. 2017

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Self-assembled redox protein nanowires have been exploited as efficient electron shuttles for an oxygen-tolerant hydrogenase.Anintra/inter-protein electron transfer chain has been achieved between the iron-sulfur centers of rubredoxin and the FeSc luster of [NiFe] hydrogenases.[ NiFe] Hydrogenases entrapped in the intricated matrix of metalloprotein nanowires achieve as table,m ediated bioelectrocatalytic oxidation of H 2 at low-overpotential.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

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A H 2 /O 2 enzymatic fuel cell as a sustainable power for a wireless device

Cited by 35 publications

References 26 publications

Impact of Carbon Nanotube Surface Chemistry on Hydrogen Oxidation by Membrane‐Bound Oxygen‐Tolerant Hydrogenases

Impact of Carbon Nanotube Surface Chemistry on Hydrogen Oxidation by Membrane‐Bound Oxygen‐Tolerant Hydrogenases

Single-use paper-based hydrogen fuel cells for point-of-care diagnostic applications

Interprotein Electron Transfer between FeS‐Protein Nanowires and Oxygen‐Tolerant NiFe Hydrogenase

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