Affiliation:
1. Department of Biology, University of Waterloo, 200 University Avenue West, Waterloo, Ontario N2L 3G1, Canada
Abstract
ABSTRACT
An NADH oxidase from the anaerobic hyperthermophilic bacterium
Thermotoga maritima
was purified. The enzyme was very active in catalyzing the reduction of oxygen to hydrogen peroxide with an optimal pH value of 7 at 80°C. The
V
max
was 230 ± 14 μmol/min/mg (
k
cat
/
K
m
= 548,000 min
−1
mM
−1
), and the
K
m
values for NADH and oxygen were 42 ± 3 and 43 ± 4 μM, respectively. The NADH oxidase was a heterodimeric flavoprotein with two subunits with molecular masses of 54 kDa and 46 kDa. Its gene sequences were identified, and the enzyme might represent a new type of NADH oxidase in anaerobes. An NADH-dependent peroxidase with a specific activity of 0.1 U/mg was also present in the cell extract of
T. maritima
.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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