Theoretical Studies on Models of the Active Site of Carbonic Anhydrase

Theoretical ab initio pseudopotential SCF computations performed on a model of the Glu 106 – Thr 199 – water H-bonded chain, free and bound to the zinc cation at the active site of carbonic anhydrase show that whereas the Glu – Thr – water form of the unbound chain is stable, the same chain, when bound to zinc, is more stable in the Glu - Thr - OH form, and the proton-relay process to that form occurs with no barrier.