Title : A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate.

Pub. Date : 1984 Jul 17

PMID : 6331509






5 Functional Relationships(s)
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1 A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide. Cyanides myeloperoxidase Homo sapiens
2 The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme. Cyanides myeloperoxidase Homo sapiens
3 The binding of cyanide to myeloperoxidase (k1 = (1.30 +/- 0.05) X 10(6) M-1 X s-1) is also regulated by an acid/base group with a pKa of 4.00 +/- 0.05 as is the case with hydrogen peroxide; also, only the protonated uncharged form of cyanide reacts with the enzyme. Cyanides myeloperoxidase Homo sapiens
4 From their effects on the binding of cyanide to the enzyme it is concluded that chloride and thiocyanate bind to myeloperoxidase only when the acid/base group is protonated. Cyanides myeloperoxidase Homo sapiens
5 The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide. Cyanides myeloperoxidase Homo sapiens