Open AccessPurification and characterization of ATPase from Nitrobacter winogradskyi
Author(s) -
Hara Tadashi,
Villobos Annabelle P.,
Fukumori Yoshihiro,
Yamanaka Tateo
Publication year - 1991
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.1574-6968.1991.tb04838.x
Subject(s) - nitrobacter , atpase , chemistry , microbiology and biotechnology , biochemistry , biology , nitrification , enzyme , organic chemistry , nitrogen
An ATPase was purified from Nitrobacter winogradskyi , and some of its molecular and enzymatic properties were determined. The enzyme was composed of two subunits of 64 and 59 kDa, respectively. The enzyme had its pH optimum at 9.5 and showed a specific activity of 7 units per mg protein. This activity was about 14% and 18% of that of F 1 ‐ATPases obtained from Escherichia coli and Sulfolobus acidocaldarius , respectively. The enzyme was 29% and 6% inhibited by 100 μM dicyclohexylcarbodiimide (DCCD) and 100 μM NaN 3 , respectively. It was not inhibited by 20 mM NaNO 3 .