10612596

Source:http://linkedlifedata.com/resource/pubmed/id/10612596

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0016948, umls-concept:C0182400, umls-concept:C0439807, umls-concept:C0441712
pubmed:issue	23
pubmed:dateCreated	2000-1-13
pubmed:abstractText	Processing of trans-2-phenylcyclopropylmethanols 5 and 6 by the monocopper/tyrosine radical enzyme galactose oxidase led to mechanism-based inactivation with a partition ratio, (k(cat) + k(inact))/k(inact), of approximately 1 and a primary deuterium isotope effect, k(inact(H))/k(inact(D)), of 3.2. The data are consistent with a radical mechanism for galactose oxidase with a short lived ketyl radical anion intermediate.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107377
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Galactose Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Probes
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	0960-894X
pubmed:author	pubmed-author:BranchaudB PBP, pubmed-author:TurnerB EBE
pubmed:issnType	Print
pubmed:day	6
pubmed:volume	9
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	3341-6
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:10612596-Catalysis, pubmed-meshheading:10612596-Galactose Oxidase, pubmed-meshheading:10612596-Kinetics, pubmed-meshheading:10612596-Molecular Probes
pubmed:year	1999
pubmed:articleTitle	Probing the radical mechanism of galactose oxidase using an ultrafast radical probe.
pubmed:affiliation	Department of Chemistry, University of Oregon, Eugene 97403-1253, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S.