Switch to
Predicate | Object |
---|---|
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 |
http://linkedlifedata.com/resource/pubmed/chemical/Horseradish Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Lactoperoxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/lignin peroxidase
|
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-meshheading:8457545-Absorptiometry, Photon,
pubmed-meshheading:8457545-Animals,
pubmed-meshheading:8457545-Binding Sites,
pubmed-meshheading:8457545-Cattle,
pubmed-meshheading:8457545-Female,
pubmed-meshheading:8457545-Horseradish Peroxidase,
pubmed-meshheading:8457545-Hydrogen-Ion Concentration,
pubmed-meshheading:8457545-Lactoperoxidase,
pubmed-meshheading:8457545-Ligands,
pubmed-meshheading:8457545-Milk,
pubmed-meshheading:8457545-Oxidation-Reduction,
pubmed-meshheading:8457545-Peroxidases,
pubmed-meshheading:8457545-Protein Conformation
|
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
|