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J. Biochem, 1977, Vol. 81, No. 4 1071-1077
© 1977 Japanese Biochemical Society

research-article

Membrane-Bound Adenosine Triphosphatase of Escherichia coli

III. Effects of Sodium Azide on the Enzyme Functions1

Hiroshi KOBAYASHI2, Masatomo MAEDA and Yasuhiro ANRAKU2,3

Department of Botany, Faculty of Science, University of Tokyo Bunkyo-ku Tokyo 113

3To whom correspondence should be addressed

  1. Sodium azide and diphenyl phosphorazidate (DPPA) inhibited purified membrane-bound ATPase [coupling factor of oxidative phosphorylation; EC 3.6.1.3 [EC] [EC] ] of Escherichia coli noncompetitively with K1 values of 39 and 51 µM, respectively.
  2. Sodium azide and DPPA inhibited the activity of ATPase bound to the membrane as effectively as that of the purified enzyme.
  3. 3) The effects of sodium azide on succinate-dependent ATP synthesis, P exchange, and ATP hydrolysis reactions by the membrane vesicles were compared under the same conditions. At concentrations below 1.0 m sodium azide inhibited ATP hydrolysis, but P1-ATP exchange and ATP synthesis were almost unaffected. At 10 mM sodium azide, both P1-ATP exchange and ATP synthesis reactions were completely inhibited, probably because at this concentration, sodium azide acted as a proton-conducting uncoupler.

1This work was supported in part by a grant (048095) from the Ministry of Education, Science and Culture or Japan.

2Present address. Division of Molecular and Cellular Biology, National Jewish Hospital and Research Center, Denver, Colorado 80206, U.S.A.


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