Metal substitutions in carbonic anhydrase: A halide ion probe study

35Cl nmr line width and activity measurements are reported for the zinc, mercury and cadmium forms of bovine and human carbonic anhydrase B. The zinc data agree well with previous reports; however, there is no 35Cl nmr line broadening observed for the cadmium and mercury derivatives of the enzyme wh...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 66; no. 4; pp. 1281 - 1286
Main Authors Smith, R.J., Bryant, R.G.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 01.10.1975
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Summary:35Cl nmr line width and activity measurements are reported for the zinc, mercury and cadmium forms of bovine and human carbonic anhydrase B. The zinc data agree well with previous reports; however, there is no 35Cl nmr line broadening observed for the cadmium and mercury derivatives of the enzyme which are inactive in the presence of excess zinc. The results suggest altered coordination geometry or first coordination sphere saturation by protein ligands for the cadmium and mercury derivatives of the enzyme.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(75)90498-2