Identification and Properties of 8-Hydroxyflavin : Adenine Dinucleotide in Electron-Transferring Flavoprotein from Peptostreptococcus elsdenii

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1976
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Mayhew, Stephen G.
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European Journal of Biochemistry. 1976, 63(2), pp. 373-390. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1976.tb10239.x
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  1. A new flavin prosthetic group has been isolated in pure form from the electron-transferring flavoprotein of Peptostreptococcus elsdenii. Its structure has been established as the FAD derivative of 7-methyl-8-hydroxyisoalloxazine.
    Proof of this structure has been obtained by chemical synthesis of 7-methyl-8-hydroxyisoalloxazine models, and by stepwise degradation of the native compound to 7-methyl-8-hydroxyalloxazine. The orange chromophore is characterized by a strong absorption band with a maximum at 472 nm (ε = 41000 M-1 cm-1) and a pK at 4.8 due to the ionisation of the C(8)-OH group.

    2. The properties of a series of functionally substituted, derivatives of 8-hydroxy flavins and lumichromes have been investigated to provide a basis for interpreting the effects of pH on the spectroscopic properties of the 8-hydroxy derivatives of FAD and FMN.

    3. The 8-hydroxy derivative of FAD is bound by apo-d-amino acid oxidase; the complex shows no catalytic activity. The 8-hydroxy derivative of FMN is bound by apoflavodoxin to give a complex which has catalytic activity similar to that of native flavodoxin. The complex is reversibly reduced by dithionite, first to a relatively stable semiquinone and further to the dihydroflavin form.
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570 Biowissenschaften, Biologie
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ISO 690GHISLA, Sandro, Stephen G. MAYHEW, 1976. Identification and Properties of 8-Hydroxyflavin : Adenine Dinucleotide in Electron-Transferring Flavoprotein from Peptostreptococcus elsdenii. In: European Journal of Biochemistry. 1976, 63(2), pp. 373-390. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1976.tb10239.x
BibTex
@article{Ghisla1976Ident-7903,
  year={1976},
  doi={10.1111/j.1432-1033.1976.tb10239.x},
  title={Identification and Properties of 8-Hydroxyflavin : Adenine Dinucleotide in Electron-Transferring Flavoprotein from Peptostreptococcus elsdenii},
  number={2},
  volume={63},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={373--390},
  author={Ghisla, Sandro and Mayhew, Stephen G.}
}
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    <dcterms:abstract xml:lang="eng">1. A new flavin prosthetic group has been isolated in pure form from the electron-transferring flavoprotein of Peptostreptococcus elsdenii. Its structure has been established as the FAD derivative of 7-methyl-8-hydroxyisoalloxazine.&lt;br /&gt;Proof of this structure has been obtained by chemical synthesis of 7-methyl-8-hydroxyisoalloxazine models, and by stepwise degradation of the native compound to 7-methyl-8-hydroxyalloxazine. The orange chromophore is characterized by a strong absorption band with a maximum at 472 nm (ε = 41000 M-1 cm-1) and a pK at 4.8 due to the ionisation of the C(8)-OH group.&lt;br /&gt;&lt;br /&gt;2. The properties of a series of functionally substituted, derivatives of 8-hydroxy flavins and lumichromes have been investigated to provide a basis for interpreting the effects of pH on the spectroscopic properties of the 8-hydroxy derivatives of FAD and FMN.&lt;br /&gt;&lt;br /&gt;3. The 8-hydroxy derivative of FAD is bound by apo-d-amino acid oxidase; the complex shows no catalytic activity. The 8-hydroxy derivative of FMN is bound by apoflavodoxin to give a complex which has catalytic activity similar to that of native flavodoxin. The complex is reversibly reduced by dithionite, first to a relatively stable semiquinone and further to the dihydroflavin form.</dcterms:abstract>
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