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Originally published In Press as doi:10.1074/jbc.M101973200 on April 10, 2001

J. Biol. Chem., Vol. 276, Issue 26, 23450-23455, June 29, 2001
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Passive Entry of CO2 and Its Energy-dependent Intracellular Conversion to HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> in Cyanobacteria Are Driven by a Photosystem I-generated Delta µH+*

Dan TchernovDagger , Yael HelmanDagger , Nir KerenDagger , Boaz LuzDagger , Itzhak OhadDagger , Leonora ReinholdDagger , Teruo Ogawa§, and Aaron KaplanDagger

From the Dagger  Faculty of Science and Mathematics and The Minerva Center for Photosynthesis under Stress, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel and the § Bioscience Center, Nagoya University, Chikusa, Nagoya 464-8601, Japan

CO2 entry into Synechococcus sp. PCC7942 cells was drastically inhibited by the water channel blocker p-chloromercuriphenylsulfonic acid suggesting that CO2 uptake is, for the most part, passive via aquaporins with subsequent energy-dependent conversion to HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>. Dependence of CO2 uptake on photosynthetic electron transport via photosystem I (PSI) was confirmed by experiments with electron transport inhibitors, electron donors and acceptors, and a mutant lacking PSI activity. CO2 uptake was drastically inhibited by the uncouplers carbonyl cyanide m-chlorophenylhydrazone (CCCP) and ammonia but substantially less so by the inhibitors of ATP formation arsenate and N, N,-dicyclohexylcarbodiimide (DCCD). Thus a Delta µH+ generated by photosynthetic PSI electron transport apparently serves as the direct source of energy for CO2 uptake. Under low light intensity, the rate of CO2 uptake by a high-CO2-requiring mutant of Synechococcus sp. PCC7942, at a CO2 concentration below its threshold for CO2 fixation, was higher than that of the wild type. At saturating light intensity, net CO2 uptake was similar in the wild type and in the mutant IL-3 suggesting common limitation by the rate of conversion of CO2 to HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>. These findings are consistent with a model postulating that electron transport-dependent formation of alkaline domains on the thylakoid membrane energizes intracellular conversion of CO2 to HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>.

* This research was supported by grants from: the United States-Israel Binational Science Foundation (BSF); Program MARS2, a cooperation between the German Bundes Ministerium fur Bildung Wissenschaft, Forschung und Technologie (BMBF) and the Israeli Ministry of Science (MOS); and by the Ministry of Science and Culture of the State of Niedersachsen.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Plant Sciences, The Hebrew Univ. of Jerusalem, 91904 Jerusalem, Israel. Tel.: 972-2-6585234; Fax: 972-2-6584463; E-mail: aaronka@vms.huji.ac.il.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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