Abstract:
:The pH dependence of the apparent affinity constants of perchlorate for cobalt(II)bovine carbonic anhydrase II has been measured by electronic absorption spectroscopy. The obtained data have been analyzed in terms of the ionization of two acidic groups of CoBCAII, and the affinity of perchlorate for the two water-containing species of the enzyme have been estimated. Furthermore, the affinity constants of nitrate, perchlorate, and azide for CoBCAII in the temperature range 5 degrees C-30 degrees C have been determined by spectrophotometric titrations at pH 7. The affinity constants for these ligands decrease with increasing temperatures. The temperature dependence of binding was used to estimate the enthalpy and entropy parameters for the formation of the corresponding 1:1 adducts. The obtained results indicate that binding of these anions to the cobalt enzyme is an enthalpy driven process which is opposed by a moderate entropy change.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Moratal JM,Martínez-Ferrer MJ,Donaire A,Aznar Ldoi
10.1016/0162-0134(92)84042-lsubject
Has Abstractpub_date
1992-01-01 00:00:00pages
65-71issue
1eissn
0162-0134issn
1873-3344pii
0162-0134(92)84042-Ljournal_volume
45pub_type
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