Abstract
Spectral and kinetic characteristics of the triplet state of all-trans-retinal (3ATR) in aqueous solutions of bovine serum albumin (BSA), interphotoreceptor retinal-binding protein (IRBP), and phosphatidylcholine (PC) liposomes have been studied by nanosecond flash photolysis. In the protein solutions, the decay kinetics of 3ATP obeys the two-exponential law (with the rate constants of 5 × 105 and 5 × 104 s−1). The introduction of liposomes into the protein solutions increases the contribution of the fast component and slows it down. The corresponding concentration dependence indicates that ATR remains localized in the proteins at the PC/protein molar ratio up to 100. The introduction of oxygen into the protein solutions has no effect on the rate constant of the slow component, but accelerates the fast component and increases its contribution. The efficiency of 3ATP quenching by molecular oxygen in the protein solutions is much lower than in water and liposomes. The photoprotective role of IRBP in the retinoid cycle is discussed.
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