The reduced form of Pseudomonas aeruginosa azurin exhibits an enhanced absorbance in the UV compared to that of the oxidized protein. This enhancement has also been observed for azurins from other bacterial species and for another type I copper protein, plastocyanin. Pulsed laser excitation of the reduced azurin in the region of enhanced absorbance at 308 nm results in single photon, rapid (<30 ns) oxidation of the copper center and formation of the hydrated electron with a quantum yield of 0.05. The hydrated electron reacts in the expected manner with scavengers such as nitrous oxide, oxygen, acetone and nitromethane. In the absence of scavengers, the electron reacts with the protein, including the disulfide bond, to form the disulfide radical anion, observed at 410 nm. The overall photophysical event involves a charge‐transfer to solvent transition although the existence of intermediate states can not be excluded.
|Original language||English (US)|
|Number of pages||6|
|Journal||Photochemistry and photobiology|
|State||Published - Sep 1989|
ASJC Scopus subject areas
- Physical and Theoretical Chemistry