Open AccessCatalytic properties of Na + ‐translocating NADH:quinone oxidoreductases from Vibrio harveyi , Klebsiella pneumoniae , and Azotobacter vinelandii
Author(s) -
Fadeeva Maria S.,
Núñez Cinthia,
Bertsova Yulia V.,
Espín Guadalupe,
Bogachev Alexander V.
Publication year - 2008
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.1574-6968.2007.01015.x
Subject(s) - azotobacter vinelandii , klebsiella pneumoniae , vibrio harveyi , chemistry , enzyme , vibrio parahaemolyticus , sodium azide , biochemistry , microbiology and biotechnology , quinone , bacteria , vibrio , nitrogenase , biology , escherichia coli , organic chemistry , nitrogen fixation , nitrogen , gene , genetics
The catalytic properties of sodium‐translocating NADH:quinone oxidoreductases (Na + ‐NQRs) from the marine bacterium Vibrio harveyi , the enterobacterium Klebsiella pneumoniae , and the soil microorganism Azotobacter vinelandii have been comparatively analyzed. It is shown that these enzymes drastically differ in their affinity to sodium ions. The enzymes also possess different sensitivity to inhibitors. Na + ‐NQR from A. vinelandii is not sensitive to low 2‐ n ‐heptyl‐4‐hydroxyquinoline N‐oxide (HQNO) concentrations, while Na + ‐NQR from K. pneumoniae is fully resistant to either Ag + or N‐ethylmaleimide. All the Na + ‐NQR‐type enzymes are sensitive to diphenyliodonium, which is shown to modify the noncovalently bound FAD of the enzyme.