|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0054860,
umls-concept:C0181904,
umls-concept:C0205145,
umls-concept:C0205681,
umls-concept:C0243071,
umls-concept:C0596972,
umls-concept:C0728873,
umls-concept:C1521743,
umls-concept:C1704646,
umls-concept:C1704675,
umls-concept:C1710236,
umls-concept:C1999216,
umls-concept:C2346592,
umls-concept:C2603343
|
|
pubmed:issue |
2-3
|
|
pubmed:dateCreated |
1994-9-26
|
|
pubmed:abstractText |
The interactions of catechol (substrate), 2-hydroxy-pyridine-N-oxide (substrate analogue), and 2-bromophenol (inhibitor) with the extradiol cleaving catechol-2,3-dioxygenase from Pseudomonas putida mt-2 have been monitored through X-ray absorption spectroscopy (XAS). The analysis of the data provides details about the mode of coordination of the substrate and of the inhibitors to the active site of the enzyme.
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|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
22
|
|
pubmed:volume |
350
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
207-12
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies.
|
|
pubmed:affiliation |
Dipartimento di Chimica, Università di Firenze, Italy.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
