Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 6, Issue 5, Pages 817-823Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.5b00002
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- Ministry of Science and Technology of the R.O.C. [NSC 100-2113-M-110-001-MY3, NSC 102-2113-M-110-005-MY2]
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Cysteine (Cys) is unique due to its highly reactive thiol group. It often regulates the biological function of proteins by acting as the redox site. Despite its biological significance, however, the valence electronic structure of Cys under the aqueous environments remains unavailable. Here, we report the VUV photoelectron spectroscopy of Cys aqueous aerosols via a newly built aerosol VUV photoelectron spectroscopy apparatus. The photoelectron spectra of Cys show distinct band shapes at varying pH conditions, reflecting the altered molecular orbital characters when its dominating form changes. The ionization energy of Cys is determined to be 8.98 +/- 0.05 eV at low pH. A new feature at a binding energy of 6.97 +/- 0.05 eV is observed at high pH, suggesting that the negative charge on the thiolate group becomes the first electron to be removed upon ionization. This work implies that when Cys is involved in redox processes, the charge transfer mechanism may be entirely altered under different pH conditions.
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