Abstract
It is known that pyridoxal-5′-phosphate (PLP), the biologically active coenzymic form of the vitamin B6 compounds, can modify proteins and influence their functional states and properties [1]. Carbonyl groups of PLP interact with amino groups to produce Schiff bases. When aldimine bond of the Schiff base is reduced stable adduct (secondary amine) is formed. In this work the properties of PLP as a possible fluorescent label for proteins were studied. Time-resolved fluorescence studies and PM3 semi-empirical calculations were carried out with model compounds (P-pyridoxyl amino acids).
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References
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Gachko, G.A., Zybelt, V.K., Kivach, L.N., Maskevich, S.A., Maskevich, A.A., Zhumal Prikl. Spect. (Russ), 47 (1987) 335.
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© 1999 Springer Science+Business Media Dordrecht
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Stepuro, V., Maskevich, S. (1999). Photophysics of P-pyridoxyl amino acids. Time-resolved fluorescence study and molecular modelling. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_16
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DOI: https://doi.org/10.1007/978-94-011-4479-7_16
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5919-0
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