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Journal Article

How Escherichia Coli Is Equipped to Oxidize Hydrogen Under Different Redox Conditions

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Citation

Lukey, M. J., Parkin, A., Roessler, M. M., Murphy, B. J., Harmer, J., Palmer, T., et al. (2010). How Escherichia Coli Is Equipped to Oxidize Hydrogen Under Different Redox Conditions. The Journal of Biological Chemistry, 285(6), 3928-3938. doi:10.1074/jbc.M109.067751.


Cite as: https://hdl.handle.net/21.11116/0000-0006-A8F4-9
Abstract
The enterobacterium Escherichia coli synthesizes two H2 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 H2 oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 is O2 tolerant and can oxidize H2 in the presence of air, whereas Hyd-2 is ineffective for H2 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.