Lk. Ignatova et al., Effects of carbonic anhydrase inhibitors on proton exchange and photosynthesis in pea protoplasts, RUSS J PL P, 48(4), 2001, pp. 467-472
At concentrations of 100-200 muM, ethoxyzolamide, a lipophilic inhibitor of
carbonic anhydrase, considerably (by 60%) inhibited light-induced CO2-depe
ndent oxygen evolution in pea protoplasts at the optimum concentration of i
norganic carbon (100 muM CO2) in the medium. At the same concentrations of
the inhibitor, electron transport in isolated pea thylakoids was inhibited
only by 6-9%. Acetazolamide, a water-soluble inhibitor of carbonic anhydras
e, affected neither the rate Of CO2-dependent O-2 evolution in protoplasts
nor electron transport in thylakoid membranes. A light-dependent proton upt
ake by protoplasts was demonstrated. At pH 7.2, the induction kinetics and
the rate of proton uptake were similar to those for CO2-dependent O-2 evolu
tion. The rate of proton uptake was decreased twofold by I mM acetazolamide
. This fact agrees with the notion that a membrane-bound carbonic anhydrase
is operative in the plasma membrane of higher plant cells. A mechanism of
its functioning is suggested. Possible functions of carbonic anhydrases in
the cells Of C-3-plants are discussed.