The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Membrane-Bound Adenosine Triphosphatase of Escherichia coli
III. Effects of Sodium Azide on the Enzyme Functions
Hiroshi KOBAYASHIMasatomo MAEDAYasuhiro ANRAKU
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1977 Volume 81 Issue 4 Pages 1071-1077

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Abstract

1) Sodium azide and diphenyl phosphorazidate (DPPA) inhibited purified membrane-bound ATPase [coupling factor of oxidative phosphorylation; EC 3. 6. 1. 3] 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) The effects of sodium azide on succinate-dependent ATP synthesis, P1-ATP exchange, and ATP hydrolysis reactions by the membrane vesicles were compared under the same conditions. At concentrations below 1.0mM, sodium azide inhibited ATP hydrolysis, but P1-ATP exchange and ATP synthesis were almost unaffected. At 10mM 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.

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© The Japanese Biochemical Society
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