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Updated: Aug 15, 2026

Determining the Serum Stability of Human Adenosine Deaminase 1 Enzyme
Published on: September 27, 2024
The protonation site of amino acids for chiral recognition by adenosine
Riyo Nakanishi1, Akimasa Fujihara2
1Department of Chemistry, Osaka Metropolitan University, Osaka, 558-8585, Japan.
Abstract:
Chiral recognition between adenosine and amino acids was investigated by ultraviolet photodissociation spectroscopy of hydrogen-bonded protonated clusters at 8 K in the gas phase. The S1-S0 transitions of protonated adenosine hydrogen-bonded with lysine, glutamine, and glutamic acid were redshifted compared to that of adenosine hydrogen-bonded with protonated arginine, indicating that protonation on adenosine caused the redshift. The relative intensity of the band at 280-285 nm of protonated adenosine hydrogen-bonded with D-glutamic acid was approximately twice that of L-glutamic acid. The enantiomers of glutamic acid and glutamine were differentiated by the spectra, but the enantiomers of arginine and lysine could not be differentiated. The protonation site of amino acids required for chiral recognition by adenosine was the α-amino group.
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