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Invited Speaker

Nature’s way to exploit hydrogen as alternative fuel

Oliver Lenz1
1 Institut für Biologie / Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, 10115 Berlin, Germany, oliver.lenz@cms.hu-berlin.de

Abstract

More than two billion years ago, ancient microbes already started to benefit from H2 that, until today, serves either as valuable energy source or as a safety valve to liberate excessive reducing power. Both the formation and consumption of H2 are catalysed by hydrogenases, which are fascinating biocatalysts exhibiting H2-conversion rates of up to 10,000 molecules per second. All hydrogenases known so far utilise abundant transition metals such as nickel and iron for catalysis, contrary to man-made H2 catalysts that predominantly rely on the rare precious metal platinum. This situation currently boosts the research on biological and bioinspired H2-catalysts. Since transition metals are intrinsically susceptible to dioxygen, the catalytic centers of most hydrogenases become inactivated or even destroyed upon interaction with O2. This property restricts the application of these biocatalysts to anaerobic conditions.

However, some microorganisms are able to gain energy from the controlled combustion of H2 with dioxygen. This process is mediated by so-called “oxygen-tolerant” [NiFe]-hydrogenases. In this context, O2 tolerance is defined as the sustained H2 cycling in presence of O2. In my seminar, I will briefly introduce the fundamental aspects of how certain [NiFe]-hydrogenases cope with the detrimental effects of O2. The second part is dedicated to the application of O2-tolerant hydrogenases in enzymatic fuel cells and light-driven H2 production.

References

Goris, T., A. F. Wait, M. Saggu, J. Fritsch, N. Heidary, M. Stein, I. Zebger, F. Lendzian, F. A. Armstrong, B. Friedrich & O. Lenz. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nat. Chem Biol. 7:310-318 (2011).

Friedrich, B., J. Fritsch & O. Lenz. Oxygen-tolerant hydrogenases in hydrogen-based technologies. Curr. Opin. Biotechnol. 22:358-364 (2011).

Lenz, O., Ludwig, M., Schubert, T., Bürstel, I., Ganskow, S., Goris, T., Schwarze, A., Friedrich, B. H2 conversion in the presence of O2 as performed by the membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha. Chem. Phys. Chem. 11: 1107-1119 (2010).

Krassen, H., Schwarze, A., Friedrich, B., Ataka, K., Lenz, O. & Heberle, J.. Photosynthetic hydrogen production by a hybrid complex of photosystem I and [NiFe]-hydrogenase. ACS Nano. 22: 4055-4061 (2009).

Cracknell, J.A., Wait, A. F., Lenz, O., Friedrich, B., Armstrong, F.A. A kinetic and thermodynamic understanding of O2 tolerance in [NiFe]-hydrogenases. Proc. Natl. Acad. Sci. U. S. A.106:20681-20686 (2009).

Vincent, K. A., J. A. Cracknell, O. Lenz, I. Zebger, B. Friedrich & F. A. Armstrong. Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. Proc. Natl. Acad. Sci. U. S. A. 102:16951-16954 (2005).

DOI®: 10.3288/contoo.paper.1450
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