The reaction of red blood cell catalase with perchlorate

Irit Aviram*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Sodium perchlorate forms a reversible and enzymatically inactive complex with human red blood cell catalase. The rates of binding and association constants increase inversely with pH. Analysis of the dependence of association constants on pH suggests participation of a carboxylate or imidazole group in the proton-assisted binding of perchlorate to catalase. Formation of the complex resulting from binding of perchlorate to the apoprotein involves a conformation change and is accompanied by alterations in the optical spectrum of catalase. In the presence of hydrogen peroxide the progressive inhibition of the enzyme by perchlorate is faster than at nonturnover conditions, indicating additional reaction of the ligand with catalase intermediate complexes.

Original languageEnglish
Pages (from-to)352-357
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - 1980


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