Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets

Lazarus, O., Woolerton, T. W., Parkin, A., Lukey, M. J., Reisner, E., Seravalli, J., Pierce, E., Ragsdale, S. W., Sargent, F., Armstrong, F. A. (October 2009) Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets. J Am Chem Soc, 131 (40). pp. 14154-5. ISSN 1520-5126

Abstract

The water-gas shift (WGS) reaction (CO + H(2)O <==> CO(2) + H(2)) is of major industrial significance in the production of H(2) from hydrocarbon sources. High temperatures are required, typically in excess of 200 degrees C, using d-metal catalysts on oxide supports. In our study the WGS process is separated into two half-cell electrochemical reactions (H(+) reduction and CO oxidation), catalyzed by enzymes attached to a conducting particle. The H(+) reduction reaction is catalyzed by a hydrogenase, Hyd-2, from Escherichia coli, and CO oxidation is catalyzed by a carbon monoxide dehydrogenase (CODH I) from Carboxydothermus hydrogenoformans. This results in a highly efficient heterogeneous catalyst with a turnover frequency, at 30 degrees C, of at least 2.5 s(-1) per minimum functional unit (a CODH/Hyd-2 pair) which is comparable to conventional high-temperature catalysts.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
organism description > bacteria > escherichia coli
CSHL Authors:
Communities: CSHL labs > Lukey lab
Depositing User: Adrian Gomez
Date: 14 October 2009
Date Deposited: 27 Jan 2020 17:06
Last Modified: 27 Jan 2020 17:06
PMCID: PMC4893959
Related URLs:
URI: https://repository.cshl.edu/id/eprint/38934

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