Open AccessDenitrification enzymes of Bacillus stearothermophilus
Author(s) -
Ho Tay P.,
Jones Alison M.,
Hollocher Thomas C.
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb06563.x
Subject(s) - enzyme , biochemistry , biology , geobacillus stearothermophilus , microbiology and biotechnology , chemistry , thermophile
The reductases of the denitrification pathway of Bacillus stearothermophilus , a thermophilic denitrifier, were surveyed in vitro. Nitrate, nitrite and nitric oxide reductases were found to be membrane‐bound, and nitrite reductase may be a copper‐containing enzyme by virtue of its rapid inactivation by the chelator, diethyldithiocarbamate. Nitric oxide reductase exhibited an optimal rate at about pH 7 rather than 5.0–5.5, as expected from the enzyme utilized by several mesophiles. Nitrous oxide reductase was not detected in assays employing reduced benzyl or methyl viologen, in spite of the appreciable N 2 O‐uptake activity of intact cells.