pH-induced protonation of lysine in aqueous solution causes chemical shifts in X-ray photoelectron spectroscopy.
We demonstrate the applicability of X-ray photoelectron spectroscopy to obtain charge- and site-specific electronic structural information of biomolecules in aqueous solution. Changing the pH of an aqueous solution of lysine from basic to acidic results in nitrogen 1s and carbon 1s chemical shifts to higher binding energies. These shifts are associated with the sequential protonation of the two amino groups, which affects both charge state and hydrogen bonding to the surrounding water molecules. The N1s chemical shift is 2.2 eV, and for carbon atoms directly neighboring a nitrogen the shift for C1s is approximately 0.4 eV. The experimental binding energies agree reasonably with our calculated energies of lysine(aq) for different pH values.
Nolting
Dirk
D
Max-Born-Institut für Nichtlineare Optik und Kurzzeitspektroskopie, Max-Born-Strasse 2a, D-12489 Berlin, Germany. nolting@mbi-berlin.de
Aziz
Emad F
EF
Ottosson
Niklas
N
Faubel
Manfred
M
Hertel
Ingolf V
IV
Winter
Bernd
B
D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000737:chemistry*; D015394:Molecular Structure; D011522:Protons; D012015:Reference Standards; D012996:Solutions / Q000737:chemistry; D013053:Spectrophotometry / Q000379:methods / Q000592:standards*; D014867:Water / Q000737:chemistry; D014965:X-Rays
D011522:Protons; D012996:Solutions; D014867:Water; D008239:Lysine