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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5182
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pubmed:dateCreated |
1994-11-8
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pubmed:abstractText |
Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.
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pubmed:grant |
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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 |
Oct
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
110-4
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7939628-Benzoate 4-Monooxygenase,
pubmed-meshheading:7939628-Binding Sites,
pubmed-meshheading:7939628-Catalysis,
pubmed-meshheading:7939628-Computer Graphics,
pubmed-meshheading:7939628-Flavin-Adenine Dinucleotide,
pubmed-meshheading:7939628-Flavins,
pubmed-meshheading:7939628-Hydrogen Bonding,
pubmed-meshheading:7939628-Mixed Function Oxygenases,
pubmed-meshheading:7939628-Models, Molecular,
pubmed-meshheading:7939628-Molecular Conformation,
pubmed-meshheading:7939628-Oxidation-Reduction,
pubmed-meshheading:7939628-Parabens,
pubmed-meshheading:7939628-Protein Conformation
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pubmed:year |
1994
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pubmed:articleTitle |
The mobile flavin of 4-OH benzoate hydroxylase.
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pubmed:affiliation |
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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