PMID: 2508759Oct 19, 1989Paper

The role of the metal ion in the refolding of denatured bovine Co(II)-carbonic anhydrase II

Biochimica Et Biophysica Acta
N Bergenhem, U Carlsson

Abstract

Conditions for reactivation of guanidine-HCl-denatured bovine Co(II)-carbonic anhydrase II are given. The renaturation is accompanied by recovery of the native Co(II)-spectrum of the enzyme. After studying the kinetics of the renaturation process, the metal ion involvement in the refolding pathway can be summarized as follows: (1) Formation of an inactive Co(II)-intermediate with the metal ion firmly bound. No native Co(II)-spectrum is observed in this state, probably due to octahedral coordination of the metal ion in this intermediate. (2) Formation of an inactive Co(II)-intermediate with a native Co(II)-spectrum. The final tetrahedral coordination of the metal ion seems to have been formed in this state. (3) Formation of the active conformation of the enzyme. A functioning active-site is formed after some rearrangements of the polypeptide chain. This isomerisation step does not need to be preceded by formation of the intermediate with a native Co(II)-spectrum. Coordination of Co2+ in a native-like manner is, however, a prerequisite for enzymic activity. It is tentatively suggested that the metal ion is involved in stabilizing a nucleation structure formed at the bottom of the active centre. This probably occurs through bindin...Continue Reading

References

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Citations

Jan 9, 1999·The Journal of Biological Chemistry·Y DaiR H Abeles
Jan 9, 1992·Biochimica Et Biophysica Acta·L G MårtenssonU Carlsson

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