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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
2002-7-17
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pubmed:abstractText |
The H64D/V68A and H64D/V68S mutants of Myoglobin are found to oxidize thioanisole with high enantioselectivity and reactivity. These mutants are also capable of enantioselective binding of alpha-methylbenzylamine, which mimics an expected sulfoxidation intermediate. The kinetic study of the amine binding shows that the Fe-O bond cleavage in the intermediate may be the chiral discrimination step of the sulfoxidation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0002-7863
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
124
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8506-7
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pubmed:dateRevised |
2008-1-17
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pubmed:meshHeading |
pubmed-meshheading:12121073-Kinetics,
pubmed-meshheading:12121073-Models, Molecular,
pubmed-meshheading:12121073-Myoglobin,
pubmed-meshheading:12121073-Phenethylamines,
pubmed-meshheading:12121073-Protein Binding,
pubmed-meshheading:12121073-Stereoisomerism,
pubmed-meshheading:12121073-Substrate Specificity,
pubmed-meshheading:12121073-Sulfides,
pubmed-meshheading:12121073-Sulfoxides,
pubmed-meshheading:12121073-Thermodynamics
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pubmed:year |
2002
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pubmed:articleTitle |
Asymmetric sulfoxidation and amine binding by H64D/V68A and H64D/V68S Mb: mechanistic insight into the chiral discrimination step.
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pubmed:affiliation |
Department of Structural Molecular Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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