The formation and properties of cobalt (III) carbonic anhydrase

Hadassah Shinar*, Gil Navon

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Cobalt (III) bovine carbonic anhydrase B was prepared by the oxidation of the corresponding cobalt (II) enzyme with hydrogen peroxide. The cobalt (III) enzyme was found to be inactive towards the hydration of carbon dioxide and the hydrolysis of p-nitrophenyl acetate. The oxidation reaction is considerably slowed down in the presence of various anion and sulfonamide inhibitors of carbonic anhydrase. The oxidation products have characteristic absorption spectra indicating direct binding of the anion inhibitors to the metal ion in the cobalt (III) carbonic anhydrase.

Original languageEnglish
Pages (from-to)471-475
Number of pages5
JournalBBA - Enzymology
Volume334
Issue number2
DOIs
StatePublished - 21 Feb 1974

Funding

FundersFunder number
Division of Basic Research, Israel Academy of Sciences and Humanitms

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