Linked Life Data

1847381

Source:http://linkedlifedata.com/resource/pubmed/id/1847381

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-3-27
pubmed:abstractText
Salicylhydroxamic and benzohydroxamic acids were found to bind to the resting state of myeloperoxidase and inhibit ligand binding to the heme iron. An ionizable group on the enzyme with pKa = 4 affects salicylhydroxamic acid binding; binding occurs when this group is not protonated. The binding of the heme iron ligands (e.g. cyanide, nitrite, and chloride) is probably controlled by the same ionizable group. The equilibrium dissociation constant of the salicylhydroxamic acid-myeloperoxidase complex is about 2 x 10(-6) M, and the association rate constant is 7.4 x 10(6) M-1.s-1. Salicylhydroxamic acid serves as a donor to the higher oxidation state of myeloperoxidase and thereby inhibits guaiacol oxidation. Salicylhydroxamic acid was also found to bind to intestinal peroxidase and lactoperoxidase. Salicylhydroxamic acid binding to all three mammalian peroxidases was about 3 orders of magnitude stronger than benzohydroxamic acid binding. We conclude that the salicylhydroxamic and benzohydroxamic acids bind in the distal heme cavity of these peroxidases and interact with the heme ligand binding site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3611-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Salicylhydroxamic acid inhibits myeloperoxidase activity.
pubmed:affiliation
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106-4901.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.