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Structure of cobalt carbonic anhydrase complexed with bicarbonate.

Håkansson K, Wehnert A
J Mol Biol 228 1212-8 (1992)
Cited: 33 times
EuropePMC logo PMID: 1474587

Abstract

The three-dimensional structure of a complex between catalytically active cobalt(II) substituted human carbonic anhydrase II and its substrate bicarbonate was determined by X-ray crystallography (1.9 A). One water molecule and two bicarbonate oxygen atoms are found at distances between 2.3 and 2.5 A from the cobalt ion in addition to the three histidyl ligands contributed by the peptide chain. The tetrahedral geometry around the metal ion in the native enzyme with a single water molecule 2.0 A from the metal is therefore lost. The geometry is difficult to classify but might best be described as distorted octahedral. The structure is suggested to represent a water-bicarbonate exchange state relevant also for native carbonic anhydrase, where the two unprotonized oxygen atoms of the substrate are bound in a carboxylate binding site and the hydroxyl group is free to move closer to the metal thereby replacing the metal-bound water molecule. A reaction mechanism based on crystallographically determined enzyme-ligand complexes is represented.

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Related citations provided by authors (1)

  1. Structure of Native and Apo Carbonic Anhydrase II and Structure of Some of its Anion-Ligand Complexes. Hakansson K, Carlsson M, Svensson LA, Liljas A J. Mol. Biol. 227 1192- (1992)

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