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Journal Article

Photophysical properties of popular fluorescent adenosine nucleotide analogs used in enzyme mechanism probing

MPS-Authors
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Leskovar,  Adriane
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Reinstein,  Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://www.sciencedirect.com/science/article/pii/S0003986108001094/pdfft?md5=f0a3eeafba8800fe529247a8df9504a8&pid=1-s2.0-S0003986108001094-main.pdf
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http://dx.doi.org/10.1016/j.abb.2008.02.035
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Citation

Leskovar, A., & Reinstein, J. (2008). Photophysical properties of popular fluorescent adenosine nucleotide analogs used in enzyme mechanism probing. Archives of Biochemistry and Biophysics, 473(1), 16-24. doi:10.1016/j.abb.2008.02.035.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-067A-A
Abstract
Fluorescent nucleotide analogs are widely used in mechanistic studies of nucleotide binding and utilizing proteins. We describe here an overview of the photophysical parameters of the most popular nucleotide analogs that have a fluorescent N-methylanthraniloyl-group attached at various positions of the nucleotide. Steady state absorption and fluorescence spectra of free chromophores depend on the type of modification (ribose, base or phosphate moiety) and the addition of proteins suggests that the labeled nucleotides also vary in sensitivity depending upon their local protein environment. Fluorescence lifetime measurements imply two to three lifetimes for each nucleotide with complex changes in dependence on solvent but more importantly also on the protein. The measured quantum yields quantify the increase in fluorescence for (C8)-MABA-ADP, MANT-ATP and (Pgamma)-MABA-ATP as 153%, 93% and 14% when bound to DnaK, ClpB and Trap1, respectively, compared to free in buffer solution.