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

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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: http://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.