Linked Life Data

8060341

Source:http://linkedlifedata.com/resource/pubmed/id/8060341

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-9-12
pubmed:abstractText
Catalytically active monoamine oxidase (MAO) is believed to exist as a dimer with each subunit containing a covalently attached flavin cofactor. Fluorescence spectroscopy performed on the resting state enzyme resulted in two separate fluorescence emissions at 480 nm and 530 nm with excitation maxima at lambda ex = 412 nm and lambda ex = 450 nm, respectively. Inactivation of MAO with pargyline resulted in concomitant loss of the absorbance at 450 nm without change in the 412 nm absorption; there also was a decrease in the emission intensity at 530 nm, while the emission at 480 nm remained unchanged. The 480 nm emission decreased and the 530 nm emission intensity increased, when the enzyme was heat denatured in the presence of NaDodSO4. From these results, it is clear that there are two different chromophores present in the resting state enzyme; the 530 nm chromophore is consistent with an oxidized flavin, while the 480 nm chromophore could be a flavin semiquinone.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
202
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1574-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Observation of two different chromophores in the resting state of monoamine oxidase B by fluorescence spectroscopy.
pubmed:affiliation
Department of Chemistry, Northwestern University, Evanston, Illinois 60208-3113.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.