| pubmed-article:1338973 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1338973 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:1338973 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1338973 | lifeskim:mentions | umls-concept:C0012727 | lld:lifeskim |
| pubmed-article:1338973 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:1338973 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1338973 | pubmed:dateCreated | 1993-7-2 | lld:pubmed |
| pubmed-article:1338973 | pubmed:abstractText | Flavocytochrome b2 (or L-lactate dehydrogenase) from baker's yeast is thought to operate by the initial formation of a carbanion, as do the evolutionarily related alpha-hydroxy acid-oxidizing FMN-dependent oxidases. Previous work has shown that, in the active site of the unligated reduced flavocytochrome b2, the group that has captured the substrate alpha-proton has a high pKapp, calculated to lie around 15 through the use of Eigen's equation. A detailed inspection of the now known three-dimensional structure of the enzyme leads to the conclusion that the high pKa belongs to His 373, an active site group that plays the role of general base in the forward reaction and of general acid in the reverse direction. Moreover, consideration of the kinetics of proton transfer during the catalytic cycle suggests that the pKa of the reduced FMN N5 position should be lowered by several pH units compared to its pKa of 20 or more when free. The features of the three-dimensional structure possibly responsible for these pK shifts are analyzed; they are proposed to consist of a network of hydrogen bonds with the solvent and of a mutual electrostatic stabilization of anionic reduced flavin and the imidazolium ion. Finally, it is suggested that similar pK shifts affect the active sites of the alpha-hydroxy acid-oxidizing flavooxidases, which are homologous to flavocytochrome b2. The functional significance of these pK shifts in terms of catalysis and semiquinone stabilization is discussed. | lld:pubmed |
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| pubmed-article:1338973 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1338973 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1338973 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1338973 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1338973 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1338973 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:1338973 | pubmed:author | pubmed-author:LedererFF | lld:pubmed |
| pubmed-article:1338973 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1338973 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:1338973 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1338973 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1338973 | pubmed:pagination | 540-8 | lld:pubmed |
| pubmed-article:1338973 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1338973 | pubmed:meshHeading | pubmed-meshheading:1338973-... | lld:pubmed |
| pubmed-article:1338973 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1338973 | pubmed:articleTitle | Extreme pKa displacements at the active sites of FMN-dependent alpha-hydroxy acid-oxidizing enzymes. | lld:pubmed |
| pubmed-article:1338973 | pubmed:affiliation | CNRS URA 1461, Hôpital Necker, Paris, France. | lld:pubmed |
| pubmed-article:1338973 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1338973 | pubmed:publicationType | Comparative Study | lld:pubmed |
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