Linked Life Data

8132563

Source:http://linkedlifedata.com/resource/pubmed/id/8132563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1994-4-18
pubmed:abstractText
Binding of aromatic substrate molecules to myeloperoxidase has been investigated by EPR spectroscopy and model building. Binding of aromatic substrate molecules, such as phenol, p-cresol, resorcinol, and 4-amino salicylate, replaces the original rhombic high spin EPR spectrum of the ferric enzyme (g = 6.74, 5.18, and 1.97) by another high spin signal (g = 7.04, 4.87, and 1.93) indicating that these substrate molecules bind near the heme center of the enzyme. Salicylhydroxamic acid and benzohydroxamic acid complexes of myeloperoxidase showed EPR spectra composed of high spin (g = 6.99, 4.93, and 1.95) and low spin (2.66, 2.22, and 1.81) signals. The hydroxamic side chains of these two substrates seem to interact with the heme iron. Model building based on the three-dimensional structure of the enzyme (Zeng, J., and Fenna, R. E. (1992) J. Mol. Biol. 226, 185-207) revealed the presence of a hydrophobic pocket at the entrance of the distal heme cavity where the aromatic ring of these substrates can bind. Moreover, the six-membered ring portion of salicylhydroxamic acid and benzohydroxamic acid could bind to this hydrophobic pocket with the hydroxamic side chain placed between the imidazole of the distal His and the heme iron. The EPR results on lactoperoxidase and intestinal peroxidase also suggest the presence of an aromatic substrate binding site similar to that of myeloperoxidase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8388-92
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase.
pubmed:affiliation
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106-4970.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't