Esterase activity of CF1 coupling factor isolated from spinach chloroplasts

Mykhailenko, NF, 1Semenikhin, AV, 1Khomochkin, AP, 1Zolotareva, EK
1M. G. Kholodhy Institute of Botany of the NAS of Ukraine, Kyiv
Dopov. Nac. akad. nauk Ukr. 2017, 3:92-98
https://doi.org/10.15407/dopovidi2017.03.092
Section: Biochemistry
Language: Ukrainian
Abstract: 

It is shown that the isolated coupling factor CF1 (a catalytic part of the ATP synthase complex of chloroplasts) is able to catalyze the hydrolysis of p-nitrophenyl ester of acetic acid. Specific inhibitors of carbonic anhydrase, acetazolamide (AA), and ethoxyzolamide (EA) in the concentration range of 1 to 100 μM modified the esterase activity of the enzyme. AA at low concentrations (less than 5 μM) stimulated and in the range of 25-75 μM inhibited the esterase activity of CF1·1-75 μM EA caused the considerable changes in the esterase activity of CF1· AA or EA affected also the latent ATPase activity of the enzyme: in the concentration 1-25 μM activated and 30-100 μM inhibited ATP hydrolysis. These results suggest that the observed esterase activity of CF1 is related to the carbonic anhydrase function of the coupling factor and is probably necessary for the proton transfer coupled with the reactions of ATP synthesis or hydrolysis.

Keywords: carbonic anhydrase, CF1-ATPase, chloroplasts, esterase, sulfanilamide inhibitors
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