{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T14:49:36Z","timestamp":1781102976059,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"23","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1991,12]]},"abstract":"<jats:p>Cyanide is a competitive inhibitor of carbon dioxide in the vitamin K-dependent glutamate carboxylase system, which plays a central role in the function of the blood clotting cascade. The mechanism of cyanide inhibition has been obscure for some time. At pH 7.2, cyanide (pKa = 9.21) will exist in solution as hydrogen cyanide to the extent of 99%. Hydrogen cyanide is linear triatomic molecule able to serve as a surrogate for carbon dioxide at the enzyme active site. Hydrogen cyanide is an acid; it will quench the deprotonated glutamate carbanion precursor to gamma-carboxyglutamate, resulting in inhibition of the carboxylation sequence.<\/jats:p>","DOI":"10.1073\/pnas.88.23.10583","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:51:47Z","timestamp":1149061907000},"page":"10583-10585","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":5,"title":["Mechanism of cyanide inhibition of the blood-clotting, vitamin K-dependent carboxylase."],"prefix":"10.1073","volume":"88","author":[{"given":"P","family":"Dowd","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of Pittsburgh, PA 15260."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S W","family":"Ham","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Pittsburgh, PA 15260."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1991,12]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.88.23.10583","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:17:34Z","timestamp":1649855854000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.88.23.10583"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,12]]},"references-count":0,"journal-issue":{"issue":"23","published-print":{"date-parts":[[1991,12]]}},"alternative-id":["10.1073\/pnas.88.23.10583"],"URL":"https:\/\/doi.org\/10.1073\/pnas.88.23.10583","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,12]]},"assertion":[{"value":"1991-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}