Hydrated electron formation on laser excitation of P-pyridoxyl amino acids and proteins.
Evidence from a characteristic transient spectrum, its lifetime and quenching by N2O demonstrates that XeCl excimer laser excitation of the reduced form of pyridoxal 5'-phosphate bound to lysine residues will produce the hydrated electron. The phenoxyl-type radical coproduct was also observed. The results identify a useful label of protein structures for site-specific electron generation which can occur outside the region of light absorption by aromatic residues of protein. The results also represent the first observation of hydrated electron formation from flash excitation of a vitamin B6 cofactor.
Greenaway
F T
FT
Department of Chemistry, Clark University, Worcester, MA 01610.
Redmond
R W
RW
Ledbetter
J W
JW
D004583:Electrons; D005609:Free Radicals; D006207:Half-Life; D007700:Kinetics; D007834:Lasers; D008239:Lysine / Q000737:chemistry; D009585:Nitrogen Dioxide / Q000737:chemistry; D010782:Photolysis; D011506:Proteins / Q000737:chemistry; D011732:Pyridoxal Phosphate / Q000737:chemistry*; D012545:Schiff Bases; D013053:Spectrophotometry; D014867:Water / Q000737:chemistry
D005609:Free Radicals; D011506:Proteins; D012545:Schiff Bases; D014867:Water; D011732:Pyridoxal Phosphate; D008239:Lysine; D009585:Nitrogen Dioxide