Journal of Bacteriology, April 2003, p. 2680-2682, Vol. 185, No. 8
0021-9193/03/$08.00+0 DOI: 10.1128/JB.185.8.2680-2682.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
and Adriana Olczak
Department of Microbiology, The University of Georgia, Athens, Georgia 30602
Received 10 October 2002/ Accepted 27 January 2003
Hydrogen-oxidizing hydrogenase activity was detected in Helicobacter hepaticus and compared to the activity in Helicobacter pylori for characteristics associated with hydrogen uptake respiratory hydrogenases. Intact whole cells could couple H2 oxidation to oxygen uptake, and no H2 uptake was observed without oxygen available to complete the respiratory pathway. The H. hepaticus enzyme coupled H2 oxidation to reduction of many positive potential acceptors, and it underwent anaerobic or reductive activation. H. hepaticus had a strong affinity for molecular H2 (apparent Km of 2.5 µM), and microelectrode measurements on the livers of live mice demonstrated that H2 is available in the host tissue at levels 20-fold greater than the apparent whole-cell Km value.
Present address: Dept. of Microbiology, North Carolina State University, Raleigh, NC 27695.
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