rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
1980-10-21
|
pubmed:abstractText |
The resonance Raman spectra of native pyrocatechase and its benzoate and phenolate complexes were investigated by using the available lines of an argon and a krypton laser. The data provide evidence for the presence of two distinct tyrosines coordinated to the active-site iron. The two tyrosines exhibit different upsilon CO values which show maximum resonance enhancements at different excitation wavelengths. Moreover, one tyrosine is more susceptible to changes in the active-site environment. Pyrocatechase is the only example thus far among iron-tyrosinate proteins where the tyrosines coordinating the iron are distinguishable.
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0006-2960
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
19
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2588-93
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7397092-Benzoates,
pubmed-meshheading:7397092-Catechol 1,2-Dioxygenase,
pubmed-meshheading:7397092-Catechols,
pubmed-meshheading:7397092-Circular Dichroism,
pubmed-meshheading:7397092-Dioxygenases,
pubmed-meshheading:7397092-Oxygenases,
pubmed-meshheading:7397092-Phenols,
pubmed-meshheading:7397092-Protein Binding,
pubmed-meshheading:7397092-Protein Conformation,
pubmed-meshheading:7397092-Protocatechuate-3,4-Dioxygenase,
pubmed-meshheading:7397092-Pseudomonas,
pubmed-meshheading:7397092-Spectrophotometry,
pubmed-meshheading:7397092-Spectrum Analysis, Raman
|
pubmed:year |
1980
|
pubmed:articleTitle |
Resonance Raman studies of pyrocatechase-inhibitor complexes.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|