The sequestration of hydroxyl ions by C2 in liquid water: useful physiological roles for a reversible complex formation in the presence of protein catalysts.

Abstract

A second function of carbonic anhydrase (CA) isoforms has already been proposed. This involves the dispersal of complexes in which six carbon dioxide molecules sequester a hydroxyl ion when the gas reacts with liquid water. The semi-catalytic reaction does not require the formation of bicarbonate as an essential corollary. This function is, therefore, a likely activity of carbonic anhydrase related proteins that have recently been discovered and which lack the active zinc site essential for the hydration of carbon dioxide. Re-examination of possible functions for the complex of six CO2 molecules with a hydroxyl anion have brought to light several circumstances where the presence of fully reversible complexes could have physiological advantages. A catalytic synthesis and dissolution of the complexes could thus be the important function for the carbonic anhydrase-related proteins (CA-RP) molecules as well as of some CA isoforms. The possible mechanisms for this extended second catalytic function and examples are briefly discussed.