Exploring Redox Properties of Aromatic Amino Acids in Water: Contrasting Single Photon vs Resonant Multiphoton Ionization in Aqueous Solutions. Roy, A., Seidel, R., Kumar, G., & Bradforth, S. E. The Journal of Physical Chemistry B, 122(14):3723–3733, American Chemical Society (ACS), 2018. 
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Paper doi abstract bibtex Direct measurements of the valence ionization energies and the reorganization energies of the three aromatic amino acids, l-tyrosine, l-tryptophan, and l-phenylalanine, in aqueous solution using the liquid microjet technique and two different photoemission methods—X-ray photoelectron spectroscopy (XPS) at 175 eV photon energy and resonant two-photon ionization (R2PI) using 2 × 267 nm (2 × 4.64 eV) UV laser light—are reported. l-Tryptophan has the lowest vertical ionization energy, 7.3 eV, followed by tyrosine (7.8 eV) and phenylalanine (∼8.7 eV). Essentially, no variation in recovered orbital energies is observed comparing near threshold ionization to X-ray ionization. Superior sensitivity of the (background-free) R2PI scheme for solutions with very low solute concentration (<2 mM) is demonstrated in contrast to the single-photon XPS measurements, which often requires solute concentrations of 0.1–1 molar. This higher sensitivity along with chemical selectivity of the R2PI technique can be exploited for both spectroscopic assignment and as an analytical tool. The nature of the adiabatic ionization energy for the three aromatic amino acids has been explored by the R2PI approach and by empirically formulating the correlation between the estimated ionization onset with electronic and nuclear relaxation on the excited state surface. Our results have implications for understanding one-electron transfer within enzymes and in redox situations where (ir)reversible deprotonation occurs such as those manifest in the biochemistry of oxidation damage.
@article{Roy_2018,
doi = {10.1021/acs.jpcb.7b11762},
url = {https://doi.org/10.1021%2Facs.jpcb.7b11762},
year = 2018,
publisher = {American Chemical Society ({ACS})},
volume = {122},
number = {14},
pages = {3723--3733},
author = {Anirban Roy and Robert Seidel and Gaurav Kumar and Stephen E. Bradforth},
title = {Exploring Redox Properties of Aromatic Amino Acids in Water: Contrasting Single Photon vs Resonant Multiphoton Ionization in Aqueous Solutions},
journal = {The Journal of Physical Chemistry B},
abstract = {Direct measurements of the valence ionization energies and the reorganization energies of the three aromatic amino acids, l-tyrosine, l-tryptophan, and l-phenylalanine, in aqueous solution using the liquid microjet technique and two different photoemission methods—X-ray photoelectron spectroscopy (XPS) at 175 eV photon energy and resonant two-photon ionization (R2PI) using 2 × 267 nm (2 × 4.64 eV) UV laser light—are reported. l-Tryptophan has the lowest vertical ionization energy, 7.3 eV, followed by tyrosine (7.8 eV) and phenylalanine (∼8.7 eV). Essentially, no variation in recovered orbital energies is observed comparing near threshold ionization to X-ray ionization. Superior sensitivity of the (background-free) R2PI scheme for solutions with very low solute concentration (<2 mM) is demonstrated in contrast to the single-photon XPS measurements, which often requires solute concentrations of 0.1–1 molar. This higher sensitivity along with chemical selectivity of the R2PI technique can be exploited for both spectroscopic assignment and as an analytical tool. The nature of the adiabatic ionization energy for the three aromatic amino acids has been explored by the R2PI approach and by empirically formulating the correlation between the estimated ionization onset with electronic and nuclear relaxation on the excited state surface. Our results have implications for understanding one-electron transfer within enzymes and in redox situations where (ir)reversible deprotonation occurs such as those manifest in the biochemistry of oxidation damage.},
bibbase_note = {<img src="https://pubs.acs.org/cms/10.1021/acs.jpcb.7b11762/asset/images/medium/jp-2017-11762c_0007.gif">}
}
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