Mode of inhibition of sodium azide on H+‐ATPase of Escherichia coli

FEBS Letters

Futai, Masamitsu¹  Maeda, Masatomo¹  Noumi, Takato¹ 

[1] Department of Organic Chemistry and Biochemistry, The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567, Japan

关键词: H+-ATPase;    F1;    Uni-site catalysis;    Multi-site catalysis;    Sodium azide;    (E. Coli);    pi;    inorganic phosphate;    32Pi;    radioactive inorganic phosphate;   

DOI  :  10.1016/0014-5793(87)81526-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sodium azide inhibited multi-site (steady-state) ATPase activity of E. coli F₁ 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 F₁.

【 授权许可】

Unknown