Lukey, M. J., Parkin, A., Roessler, M. M., Murphy, B. J., Harmer, J., Palmer, T., Sargent, F., Armstrong, F. A. (February 2010) How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. J Biol Chem, 285 (6). pp. 3928-38. ISSN 1083-351X (Public Dataset)
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Abstract
The enterobacterium Escherichia coli synthesizes two H(2) uptake enzymes, Hyd-1 and Hyd-2. We show using precise electrochemical kinetic measurements that the properties of Hyd-1 and Hyd-2 contrast strikingly, and may be individually optimized to function under distinct environmental conditions. Hyd-2 is well suited for fast and efficient catalysis in more reducing environments, to the extent that in vitro it behaves as a bidirectional hydrogenase. In contrast, Hyd-1 is active for H(2) oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 is O(2) tolerant and can oxidize H(2) in the presence of air, whereas Hyd-2 is ineffective for H(2) oxidation under aerobic conditions. The results have direct relevance for physiological roles of Hyd-1 and Hyd-2, which are expressed in different phases of growth. The properties that we report suggest distinct technological applications of these contrasting enzymes.
| 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: | |
| Depositing User: | Adrian Gomez |
| Date: | 5 February 2010 |
| Date Deposited: | 27 Jan 2020 16:42 |
| Last Modified: | 27 Jan 2020 16:42 |
| PMCID: | PMC2823535 |
| Related URLs: | |
| Dataset ID: |
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| URI: | https://repository.cshl.edu/id/eprint/38939 |
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