Laser photolysis study of spectral and kinetic characteristics of the triplet state of all-trans-retinal in aqueous solutions of retinal-binding proteins and liposomes

Autor: T. C. Konstantinova, G. R. Kalamkarov, Peter P. Levin, T. F. Shevchenko, P. V. Aboltin
Rok vydání: 2013
Předmět:
Zdroj: High Energy Chemistry. 47:103-106
ISSN: 1608-3148
0018-1439
DOI: 10.1134/s0018143913030090
Popis: 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.
Databáze: OpenAIRE
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