|Title||Effect of carbonic anhydrase inhibitors on enzymatic activity of isolated thylakoid CF1 ATPase|
|Publication Type||Journal Article|
|Year of Publication||2016|
|Authors||Khomochkin, AP, Semenikhin, AV, Zolotareva, EK|
|Abbreviated Key Title||Dopov. Nac. akad. nauk Ukr.|
We studied the effect of carbonic anhydrase inhibitors — acetazolamide (AA) and ethoxyzolamide (EA) — on the enzymatic activity of the isolated coupling factor CF1 — a catalytic part of ATPsynthase complex of chloroplasts. The enzyme was isolated from spinach chloroplasts after their extraction with 1 mM EDTA. Carbonic anhydrase activity CF1, which was determined in a solution by the acceleration of the formation of CO2 in the bicarbonate dehydration reaction, was 73 μmol CO2 · (min · mg protein)-1 and almost 3 times more than the ATPase activity of the enzyme. Acetazolamide and ethoxyzolamide inhibit both the ATPase and carbonic anhydrase activities of CF1· I50 for Ca2+ -ATPase reaction catalyzed by isolated CF1 in solution was 2 μM for AA and EA. ATPase activity increased somewhat with the concentration of EA. 50% inhibition of the carbonic anhydrase activity was achieved in the presence of 2 μM AA and 12 μM EA, respectively. Thus, water-soluble AA and liposoluble EA inhibit both the ATPase and carbonic anhydrase enzyme activities at similar and relatively low concentrations. The functional role of the discovered carbonic anhydrase activity may consist in facilitating the transfer of protons uptaken or released in the reactions of ATP synthesis or hydrolysis, respectively.
|Keywords||acetazolamide, carbonic anhydrase, CF1 ATPase, hydrolysis of ATP, photosynthetic membranes of chloroplasts|
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