@article{Massey19798Merc-8392,
  year={1979},
  title={8-Mercaptoflavins as Active Site Probes of Flavoenzymes},
  number={19},
  volume={254},
  journal={Journal of Biological Chemistry},
  pages={9640--9650},
  author={Massey, Vincent and Ghisla, Sandro and Moore, Edwin G.}
}

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    <dc:creator>Ghisla, Sandro</dc:creator>
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    <dcterms:issued>1979</dcterms:issued>
    <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 254 (1979), 19, pp. 9640-9650</dcterms:bibliographicCitation>
    <dcterms:abstract xml:lang="eng">Representative examples of the various classes of flavoproteins have been converted to their apoprotein forms and the native flavin replaced by 8-mercapto- FMN or 8-mercapto-FAD. The spectral and catalytic properties of the modified enzymes are characteristically different from one group to another; the results suggest that flavin interactions at positions N (1) or N(5) of the flavin chromophore have profound influences on the properties of the flavoprotein. 1. The 8-thiolate anion form of 8-mercaptoflavin has an absorption maximum in the region 520 to 550 nm (e ~30 mM-1 cm-1). This form is retained on binding to flavoproteins whose physiological reactions involve obligatory one-electron transfers (e.g. flavodoxin, NADPH-cytochrome P-450 reductase). In the native form these enzymes stabilize the blue neutral radical of the flavin. A radical form of 8-mercaptoflavin is also stabilized by these proteins. 2. The p-quinoid form of 8-mercaptoflavin has an absorption maximum in the range 560 to 600 nm (e ~30 mM-1 cm-1). This form is stabilized on binding to flavoproteins of the dehydrogenase-oxidase class (e.g. glucose oxidase, n-amino acid oxidase, lactate oxidase, Old Yellow Enzyme). These same enzymes in their native flavin form stabilize the red semiquinone, and have a pronounced reactivity with sulfite to form flavin N(5)- sulfite adducts. These properties of the native enzyme,including the ability to react with nitroalkane carbanions, are not exhibited by the 8-mercaptoflavoproteins. 3. A group of flavoenzymes  fails to conform strictly to the above classification, exhibiting some properties of both classes. These include the examples of flavoprotein hydroxylases and transhydrogenases studied. 4. The riboflavin-binding protein of hen egg whites binds 8-mercaptoriboflavin preferentially in the unionized state, resulting in a shift in pK from 3.8 with free 8-mercaptoriboflavin to ≥ 9.0 with the protein-bound form.</dcterms:abstract>
    <dc:creator>Moore, Edwin G.</dc:creator>
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    <dc:contributor>Massey, Vincent</dc:contributor>
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    <dc:creator>Massey, Vincent</dc:creator>
    <dcterms:title>8-Mercaptoflavins as Active Site Probes of Flavoenzymes</dcterms:title>
    <dc:contributor>Moore, Edwin G.</dc:contributor>
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    <dc:contributor>Ghisla, Sandro</dc:contributor>
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