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6-Azido- and 6-aminoflavins as active-site probes of flavin enzymes

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1986

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Massey, Vincent
Yagi, Kunio

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Biochemistry. 1986, 25(24), pp. 8095-8102. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00372a045

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6-Azidoflavins have been bound to the apoproteins of five representative flavoproteins and their properties, before and after light irradiation, compared with those of the same proteins containing the appropriate 6-aminoflavin. In the dark the 6-azidoflavoproteins are quite stable, except for L-lactate oxidase, where spontaneous conversion to the 6-amino-FMN enzyme occurs slowly at pH 7. 6-Azido-FMN Old Yellow Enzyme is converted to the 6-amino-FMN enzyme by aerobic turnover with NADPH, and 6-azido-FAD D-amino acid oxidase is converted to the 6-amino-FAD enzyme by treatment with D-alanine. Light irradiation of 6-azidoriboflavin bound to riboflavin-binding protein does not result in any covalent fixation of the flavin to the protein. Light irradiation of 6-azido-FMN flavodoxin gives only a small amount of covalent linkage. In contrast, 6-azido-FMN Old Yellow Enzyme undergoes a very facile light-induced change, in which approximately 50% of the flavin is attached in a stable covalent linkage to the protein. The resulting flavoprotein form has lost the ability to bind phenols, a distinctive characteristic of the native enzyme; it does, however, bind NADPH, but the latter cannot reduce the covalently bound flavin. 6-Azido-FAD D-amino acid oxidase also undergoes a facile light modification, in which almost quantitative fixation of the flavin to the protein takes place. The resulting flavoprotein cannot bind benzoate, an active-site ligand for the native enzyme, nor is it reduced anaerobically by D-alanine. The covalent linkage is fairly labile and is destroyed on denaturation of the protein. 6-Azido-FMN lactate oxidase is also fairly susceptible to light irradiation; in this case, however, much of the change occurs in a dark reaction following irradiation. The product is readily reduced by L-lactate, in contrast to the results with D-amino acid oxidase. We have not yet been able to determine whether a covalent linkage occurs, although the evidence implies that a labile covalent linkage is formed, which is probably hydrolyzed in a subsequent dark reaction.

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570 Biowissenschaften, Biologie

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ISO 690MASSEY, Vincent, Sandro GHISLA, Kunio YAGI, 1986. 6-Azido- and 6-aminoflavins as active-site probes of flavin enzymes. In: Biochemistry. 1986, 25(24), pp. 8095-8102. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi00372a045
BibTex
@article{Massey19866Azid-8471,
  year={1986},
  doi={10.1021/bi00372a045},
  title={6-Azido- and 6-aminoflavins as active-site probes of flavin enzymes},
  number={24},
  volume={25},
  issn={0006-2960},
  journal={Biochemistry},
  pages={8095--8102},
  author={Massey, Vincent and Ghisla, Sandro and Yagi, Kunio}
}
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