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Paramagnetic 1H and 13C NMR studies on cobalt-substituted human carbonic anhydrase I carboxymethylated at active site histidine-200: molecular basis for the changes in catalytic properties induced by the modification

Autor: R G, Khalifah, J I, Rogers, P, Harmon, P J, Morely, S B, Carroll

Publikováno v: Biochemistry. 23(14)

Using bromo[1-13C]acetate to modify N tau of His-200 of human carbonic anhydrase isozyme I leads to the introduction of a useful 13C NMR probe into the active site. To complement our previous diamagnetic NMR studies with this probe, we have now succe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::727f117f890ba7268f25d8d9011f6dce
https://pubmed.ncbi.nlm.nih.gov/6432037

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