Publikation: Structure of the oxygen adduct intermediate in the bacterialluciferase reaction : 13C nuclear magnetic resonance determination
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1978
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Published
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Proceedings of the National Academy of Science of the United States of America. 1978, 75(12), pp. 5860-5863
Zusammenfassung
By using FMN enriched in 13C (90%) at position C-4a, we have conclusively shown that the reaction of molecular oxygen with bacterial luciferase-bound FMNH2 forms an adduct at the 4a position. Consistent with this are 13C NMR studies of FMN and other flavin compounds which show that this carbon should be unusually reactive in the reduced 1,5-dihydroflavins with respect to electrophilic attacks.
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
subzero temperature, oxidation-reduction, substituted flavins, flavoproteins
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ISO 690
GHISLA, Sandro, J. Woodland HASTINGS, Vincent FAVAUDON, Jean-Marc LHOSTE, 1978. Structure of the oxygen adduct intermediate in the bacterialluciferase reaction : 13C nuclear magnetic resonance determination. In: Proceedings of the National Academy of Science of the United States of America. 1978, 75(12), pp. 5860-5863BibTex
@article{Ghisla1978Struc-7556,
year={1978},
title={Structure of the oxygen adduct intermediate in the bacterialluciferase reaction : 13C nuclear magnetic resonance determination},
number={12},
volume={75},
journal={Proceedings of the National Academy of Science of the United States of America},
pages={5860--5863},
author={Ghisla, Sandro and Hastings, J. Woodland and Favaudon, Vincent and Lhoste, Jean-Marc}
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<dcterms:abstract xml:lang="eng">By using FMN enriched in 13C (90%) at position C-4a, we have conclusively shown that the reaction of molecular oxygen with bacterial luciferase-bound FMNH2 forms an adduct at the 4a position. Consistent with this are 13C NMR studies of FMN and other flavin compounds which show that this carbon should be unusually reactive in the reduced 1,5-dihydroflavins with respect to electrophilic attacks.</dcterms:abstract>
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