How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. / Lukey, M.J.; Parkin, A.; Roessler, M.M.; Murphy, B.J.; Harmer, J.; Armstrong, F.A.; Palmer, T.; Sargent, F.
In: Journal of Biological Chemistry, Vol. 285, No. 6, 05.02.2010, p. 3928-3938.Research output: Contribution to journal › Article
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TY - JOUR
T1 - How Escherichia coli is equipped to oxidize hydrogen under different redox conditions
A1 - Lukey,M.J.
A1 - Parkin,A.
A1 - Roessler,M.M.
A1 - Murphy,B.J.
A1 - Harmer,J.
A1 - Armstrong,F.A.
A1 - Palmer,T.
A1 - Sargent,F.
AU - Lukey,M.J.
AU - Parkin,A.
AU - Roessler,M.M.
AU - Murphy,B.J.
AU - Harmer,J.
AU - Armstrong,F.A.
AU - Palmer,T.
AU - Sargent,F.
PY - 2010/2/5
Y1 - 2010/2/5
N2 - The enterobacterium Escherichia coli synthesizes two H 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 oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 isO tolerant and can oxidize H in the presence of air, whereas Hyd-2 is ineffective for H 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. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
AB - The enterobacterium Escherichia coli synthesizes two H 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 oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 isO tolerant and can oxidize H in the presence of air, whereas Hyd-2 is ineffective for H 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. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
U2 - 10.1074/jbc.M109.067751
DO - 10.1074/jbc.M109.067751
M1 - Article
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 6
VL - 285
SP - 3928
EP - 3938
ER -