{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T17:19:52Z","timestamp":1771003192321,"version":"3.50.1"},"reference-count":38,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2004,2,3]],"date-time":"2004-02-03T00:00:00Z","timestamp":1075766400000},"content-version":"vor","delay-in-days":4019,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[1993,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Carbonic anhydrase is inhibited by the \u201cmetal poison\u201d cyanide. Several spectroscopic investigations of carbonic anhydrase where the natural zinc ion has been replaced by cobalt have further strengthened the view that cyanide and cyanate bind directly to the metal. We have determined the structure of human carbonic anhydrase II inhibited by cyanide and cyanate, respectively, by X\u2010ray crystallography. It is shown that the inhibitors replace a molecule of water, which forms a hydrogen bond to the peptide nitrogen of Thr\u2010199 in the native structure. The coordination of the zinc ion is hereby left unaltered compared to the native crystal structure, so that the zinc coordinates three histidines and one molecule of water or hydroxyl ion in a tetrahedral fashion. The binding site of the two inhibitors is identical to what earlier has been suggested to be the position of the substrate (CO<jats:sub>2<\/jats:sub>) when attacked by the zinc bound hydroxyl ion. The peptide chain undergoes no significant alterations upon binding of either inhibitor. \u00a9 1993 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.340150207","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T01:24:23Z","timestamp":1117329863000},"page":"177-182","source":"Crossref","is-referenced-by-count":43,"title":["Metal poison inhibition of carbonic anhydrase"],"prefix":"10.1002","volume":"15","author":[{"given":"Martin","family":"Lindahl","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L. Anders","family":"Svensson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anders","family":"Liljas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_2","first-page":"151","volume-title":"Carbonic Anhydrase","author":"Tashian R. E.","year":"1991"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.72.1.51"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1038\/newbio235131a0"},{"key":"e_1_2_1_5_2","unstructured":"Eriksson A. E. Liljas A.The refined structure of bovine carbonic anhydrase III at 2.0 \u00c5 resolution.Proteins(in press)."},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1113\/jphysiol.1933.sp003077"},{"key":"e_1_2_1_7_2","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0021-9258(18)75831-6","article-title":"The catalysis of the hydration of carbon dioxide and dehydration of carbonic acid by an enzyme isolated from red blood cells","volume":"103","author":"Stadie W. C.","year":"1933","journal-title":"J. Biol. 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Liljas A.The structure of native and apo carbonic anhydrase II and some of its anion ligand complexes.J. Mol. 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