Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1993-4-23
pubmed:abstractText
Native lactoperoxidase, compound III, and the reduced forms (at pH 6 and 9) were studied using X-ray absorption spectroscopy (XAS). Native lactoperoxidase has four pyrrole nitrogen ligands at an average distance of 2.04 +/- 0.01 A, a proximal ligand at 1.91 +/- 0.02 A, and a sixth (distal) ligand at 2.16 +/- 0.03 A. Lactoperoxidase native enzyme has a first coordination shell structure that is similar to that of native lignin peroxidase [Sinclair, R., Yamazaki, I., Bumpus, J., Brock, B., Chang, C.-S., Albo, A., & Powers, L. (1992) Biochemistry 31, 4892-4900] and different from that of horseradish peroxidase [Chance, B., Powers, L., Ching, Y., Poulos, T., Schonbaum, G., Yamazaki, I., & Paul, K. (1984) Arch. Biochem. Biophys. 235, 596-611]. Similarly, lactoperoxidase compound III resembles lignin peroxidase compound III. The five-coordinated ferrous form was stable at pH 9, but at pH 6 it was rapidly converted to the six-coordinated form with a distal ligand at 2.18 +/- 0.03 A. No evidence typical of changes in spin state was obtained at the different pH values.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2780-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
An extended X-ray absorption fine structure investigation of the structure of the active site of lactoperoxidase.
pubmed:affiliation
National Center for the Design of Molecular Function, Utah State University, Logan 84322-4630.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't