Journal
JOURNAL OF PHYSICAL CHEMISTRY C
Volume 114, Issue 27, Pages 12003-12009Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp102616m
Keywords
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Funding
- EPSRC [Supergen 5]
- BBSRC [BB/D52222X/1, BB/H003878/1]
- Merton College, Oxford
- CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior - Ministry of Education of Brazil)
- Biotechnology and Biological Sciences Research Council [BB/D52222X/1, BB/H003878/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/D047943/1, EP/H019480/1] Funding Source: researchfish
- BBSRC [BB/H003878/1] Funding Source: UKRI
- EPSRC [EP/D047943/1, EP/H019480/1] Funding Source: UKRI
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The special properties of O-2-tolerant [NiFe]-hydrogenases make it possible, in principle, to operate all-enzyme hydrogen fuel cells. These devices show unusual power characteristics, as revealed in a series of experiments in which the O-2-tolerant hydrogenase (Hyd-1) from Escherichia coli is used as H-2-oxidation catalyst (anode) and a bilirubin oxidase is used as O-2-reduction catalyst (cathode). In a fuel cell adaptable for variable fuel and oxidant supply, three limiting conditions were examined: (1) the anode and cathode separated by a Nafion membrane and 100% H-2 and 100% O-2 fed to the separate compartments, (2) a membrane-free mixed feed cell with a fuel-rich (96% H-2) hydrogen/oxygen mixture, and (3) a membrane-free mixed feed cell with a fuel-weak (4% H-2) hydrogen/air mixture. Condition (1) exposes the effect of O-2-crossover which is evident even for an O-2-tolerant hydrogenase, whereas condition (2) is limited by bilirubin oxidase activity on the cathode. Condition (3) yields power only under high-load (resistance) conditions that maintain a high output voltage; a low load collapses the power (akin to a circuit breaker) because of complete inactivation of the [NiFe]-hydrogenase when subjected to O-2 at high potential. Recovery of the hydrogen-poor fuel cell is not achieved simply by restoring the high load but by briefly connecting a second anode containing active hydrogenase which discharges electrons to provide a jump start. The second anode had remained active despite being in the same O-2 environment because it was not electrochemically connected to an oxidizing source (the cathode), thus demonstrating that, under 4% H-2, the presence of 20% O-2 does not, alone, cause hydrogenase inactivation, but simultaneous connection to an oxidizing potential is also required. The investigation helps to illuminate obstacles to the application of hydrogenases in fuel-cell technology and suggests phenomena that might be relevant for biology where biological membranes are engaged in H2 oxidation under aerobic conditions.
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