Abstract
The special properties of O2-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 O2-tolerant hydrogenase (Hyd-1) from Escherichia coli is used as H2-oxidation catalyst (anode) and a bilirubin oxidase is used as O2-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% H2 and 100% O2 fed to the separate compartments, (2) a membrane-free mixed feed cell with a fuel-rich (96% H2) hydrogen/oxygen mixture, and (3) a membrane-free mixed feed cell with a fuel-weak (4% H2) hydrogen/air mixture. Condition (1) exposes the effect of O2-crossover which is evident even for an O2-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 O2 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 O2 environment because it was not electrochemically onnected to an oxidizing source (the cathode), thus demonstrating that, under 4% H2, the presence of 20% O2 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.
Original language | English |
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Pages (from-to) | 12003 |
Number of pages | 12009 |
Journal | Journal of Physical Chemistry C |
Volume | 114 |
Issue number | 27 |
DOIs | |
Publication status | Published - 15 Jul 2010 |