Denitrification enzymes ofBacillus stearothermophilus

Autor:	Thomas C. Hollocher, Alison M. Jones, Tay P. Ho
Rok vydání:	1993
Předmět:	Denitrification Nitric-oxide reductase Chemistry Denitrification pathway Nitrous-oxide reductase Nitrite reductase Nitrate reductase Microbiology Nitric oxide chemistry.chemical_compound Biochemistry Genetics Nitrite Molecular Biology
Zdroj:	FEMS Microbiology Letters. 114:135-138
ISSN:	1574-6968 0378-1097
DOI:	10.1111/j.1574-6968.1993.tb06563.x
Popis:	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 N2O-uptake activity of intact cells.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::621a8f1588a4b32c0070b2d6d0e9ce75 https://doi.org/10.1111/j.1574-6968.1993.tb06563.x Zobrazit plný text záznamu Plný text