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Mode of inhibition of sodium azide on H + ‐ATPase of Escherichia coli
Author(s) -
Noumi Takato,
Maeda Masatomo,
Futai Masamitsu
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81526-0
Subject(s) - sodium azide , azide , chemistry , atpase , escherichia coli , cooperativity , sodium , ligand (biochemistry) , biochemistry , enzyme , organic chemistry , receptor , gene
Sodium azide inhibited multi‐site (steady‐state) ATPase activity of E. coli F 1 more than 90%, but did not affect uni‐site (single‐site) ATPase activity. Thus azide inhibited multi‐site ATPase activity by lowering catalytic cooperativity. Consistent with this observation, azide changed the ligand‐induced fluorescence response of aurovertin bound to F 1 .