scholarly journals Effect of Carbonic Anhydrase Inhibitors on Inorganic Carbon Accumulation by Chlamydomonas reinhardtii

1985 ◽  
Vol 79 (1) ◽  
pp. 177-183 ◽  
Author(s):  
James V. Moroney ◽  
H. David Husic ◽  
N. E. Tolbert
1991 ◽  
Vol 69 (5) ◽  
pp. 1079-1087 ◽  
Author(s):  
H. David Husic

In the unicellular green alga Chlamydomonas reinhardtii, a form of the enzyme carbonic anhydrase that is localized outside of the plasma membrane is an inducible component of a system that is involved in inorganic carbon acquisition and concentration from the growth medium. This article contains a review and analysis of the current literature regarding the extracellular carbonic anhydrase from Chlamydomonas reinhardtii and presents some new studies on its extracellular localization, physiological role in inorganic carbon acquisition, and some of the structural and catalytic properties of the enzyme. Key words: carbonic anhydrase, Chlamydomonas reinhardtii, inorganic carbon utilization.


1991 ◽  
Vol 69 (5) ◽  
pp. 1032-1039 ◽  
Author(s):  
M. J. Merrett

Inorganic carbon transport was investigated in a range of marine microalgae. A small-celled strain of Stichococcus bacillaris, containing appreciable carbonic anhydrase activity, showed a high affinity for CO2, while measurement of the internal inorganic carbon pool by the silicone oil layer centrifugal filtering technique showed cells concentrated inorganic carbon up to 20-fold in relation to the external medium at pH 5.0 but not pH 8.3. The addition of 14CO2 or H14CO3− to cells in short-term kinetic experiments at pH 8.3 confirmed that only CO2 provides the exogenous substrate for substantial inorganic carbon accumulation within the cell. High-affinity HCO3− transport in Phaeodactylum tricornutum and Porphyridium purpureum is dependent on sodium ions, while intracellular carbonic anhydrase increased the steady-state flux of CO2 from inside the plasmalemma to Rubisco. In the presence of HCO3− the intracellular pH in cells of P. purpureum is 7.1 but on carbon starvation the pH falls to 6.0. Ethoxyzolamide blocks bicarbonate-dependent alkalinization of the cytosol, confirming a central role for carbonic anhydrase–bicarbonate in cytosolic pH regulation. Carbonic anhydrase activity is pH dependent in P. purpureum so synergistic interaction between CO2 uptake and bicarbonate transport may occur.


1988 ◽  
Vol 88 (2) ◽  
pp. 491-496 ◽  
Author(s):  
Livingston J. Manuel ◽  
James V. Moroney

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