Hydrogen-oxidizing capabilities of Helicobacter hepaticus and in vivo availability of the substrate.
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 H(2) oxidation to oxygen uptake, and no H(2) uptake was observed without oxygen available to complete the respiratory pathway. The H. hepaticus enzyme coupled H(2) oxidation to reduction of many positive potential acceptors, and it underwent anaerobic or reductive activation. H. hepaticus had a strong affinity for molecular H(2) (apparent K(m) of 2.5 micro M), and microelectrode measurements on the livers of live mice demonstrated that H(2) is available in the host tissue at levels 20-fold greater than the apparent whole-cell K(m) value.
Maier
Robert J
RJ
Department of Microbiology, The University of Georgia, Athens, Georgia 30602, USA. rmaier@uga.edu
Olson
Jonathan
J
Olczak
Adriana
A
D000818:Animals; D005260:Female; D016998:Helicobacter / Q000201:enzymology*; D006859:Hydrogen / Q000032:analysis / Q000378:metabolism*; D006864:Hydrogenase / Q000378:metabolism*; D008099:Liver / Q000737:chemistry*; D051379:Mice; D008810:Mice, Inbred C57BL; D010084:Oxidation-Reduction; D010100:Oxygen
D006859:Hydrogen; D006864:Hydrogenase; D010100:Oxygen