Photosensitive damage of dipeptides: mechanism and influence of structure.

We illustrate the influence of the dipeptide structure on photosensitive damage and the kinetic mechanism was investigated using acenaphthenequinone (ACQ) as a triplet photosensitizer. With tyrosine (Tyr) serving as the core structure, two classic dipeptides with double (trptophan-tyrosine, Trp-Tyr) and single (tyrosine-alanine, Tyr-Ala and Ala-Tyr) active reaction sites were constructed, and the underlying photodamage mechanisms were investigated carefully. According to the experimental results, the proton-coupled electron transfer processes between ACQ and numerous Trp-Tyr reaction sites have independent reaction properties.

Investigation on the photoinduced chemical reaction between -benzoquinone and tryptophan in homogeneous solution.

Photoinduced electron transfer (PET) and energy transfer between amino acids and bioquinones have become research hotspots, due to the important roles they play in a physiological environment. However, as classic benzoquinones and amino acids, the reaction mechanism of -benzoquinone (PBQ) and tryptophan (Trp) is still unclear. In this work, the photoinduced chemical reaction of PBQ and Trp was investigated in homogeneous solution using time-resolved electron paramagnetic resonance and laser flash photolysis techniques.