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Cited by 271

The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.

Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels

Open access
Vincent, Kylie A., Cracknell, James A., Lenz, Oliver, Zebger, Ingo, Friedrich, Bärbel, Armstrong, Fraser A.·2005·Proceedings of the National Academy of Sciences

Abstract

Use of hydrogen in fuel cells requires catalysts that are tolerant to oxygen and are able to function in the presence of poisons such as carbon monoxide. Hydrogen-cycling catalysts are widespread in the bacterial world in the form of hydrogenases, enzymes with unusual active sites composed of iron, or nickel and iron, that are buried within the protein. We have established that the membrane-bound hydrogenase from the β-proteobacterium Ralstonia eutropha H16, when adsorbed at a graphite electrode, exhibits rapid electrocatalytic oxidation of hydrogen that is completely unaffected by carbon monoxide [at 0.9 bar (1 bar = 100 kPa), a 9-fold excess] and is inhibited only partially by oxygen. The practical significance of this discovery is illustrated with a simple fuel cell device, thus demonstrating the feasibility of future hydrogen-cycle technologies based on biological or biologically inspired electrocatalysts having high selectivity for hydrogen.

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Metadata

Authors
Vincent, K. A., Cracknell, J. A., Lenz, O., Zebger, I., Friedrich, B., & Armstrong, F. A.
Venue
Proceedings of the National Academy of Sciences
Published
2005-10-31
Volume
102
Issue
47
Pages
16951-16954
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1547056372
Cited by
271
References
16
FWCI
12.51
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. https://app.cochat.ai/papers/10.1073/pnas.0504499102
The paper
Vincent, K. A., Cracknell, J. A., Lenz, O., Zebger, I., Friedrich, B., & Armstrong, F. A. (2005). Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0504499102

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