Affiliation:
1. Department of Microbiology, The University of Georgia, Athens, Georgia 30602
Abstract
ABSTRACT
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 μM), 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
29 articles.
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