Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

• Published in: FEBS letters 2004-11, Vol.577 (1), p.305-308
• Main Authors: Khristin, M.S., Ignatova, L.K., Rudenko, N.N., Ivanov, B.N., Klimov, V.V.
• Format: Article
• Language: English
• Subjects: C 3-plant; C3-plant; CA, carbonic anhydrase; Carbonic anhydrase; Carbonic Anhydrases - metabolism; Chl, chlorophyll; Chloroplast; Core complex; CP43 and CP47, chlorophyll-binding proteins with molecular weights 43 and 47 kDa, respectively; DM, n-dodecyl-β-maltoside; Electrophoresis, Polyacrylamide Gel; EZ, ethoxyzolamide; LHC, light-harvesting complex; mafenide, p-aminomethylbenzenesulfonamide; Photosystem II; Photosystem II Protein Complex - metabolism; Plants - enzymology; PSII, photosystem II
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2004.10.001

The thylakoid membrane containing photosystem II (PSII membranes) from pea and wheat leaves catalyzed the reaction of CO 2 hydration with low rate, which increased after their incubation either with Triton X-100, up to Triton/chlorophyll ratio 1:1, or 1 M CaCl 2. The presence of the inhibitor of CAs, p-aminomethylbenzensulfonamide (mafenide), at the start line in the course of electrophoresis of PSII membranes solubilized by n-dodecyl-β-maltoside (DM) decreased the amount of PSII core complex in the gel. The elution of PSII core complex from the column with immobilized mafenide occurred only either by mafenide or another inhibitor of CAs, ethoxyzolamide. The above results led to a conclusion that membrane-bound CA activity associated with PSII is situated in the core complex.