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MECHANISM OF CYANIDE INHIBITION OF THE BLOOD-CLOTTING, VITAMIN-K-DEPENDENT CARBOXYLASE
- Authors
- Dowd, Paul; Ham, Seung-Wook
- Issue Date
- Dec-1991
- Publisher
- NATL ACAD SCIENCES
- Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.88, no.23, pp 10583 - 10585
- Pages
- 3
- Journal Title
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Volume
- 88
- Number
- 23
- Start Page
- 10583
- End Page
- 10585
- ISSN
- 0027-8424
1091-6490
- Abstract
- 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 (pK(a) = 9.21) will exist in solution as hydrogen cyanide to the extent of 99%. Hydrogen cyanide is a 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.
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