Abstract
The kinetics of quenching of the all-trans-retinal triplet state by air oxygen in aqueous solutions of bovine serum albumin and in a cardiolipin liposome suspension was investigated by nanosecond laser photolysis. It was established that the quenching reaction rate constant in the albumin solution (1.8 × 108 l mol−1 s−1) was an order of magnitude less than in liposomes (3.1 × 109 l mol−1 s−1). These constants were 5.0 × 109 and 1.1 × 109 l mol−1 s−1 in methanol and aqueous solutions containing 10 vol % methanol, respectively. The effect of hindered oxygen access to the Lall-trans-retinal attached to albumin is discussed in terms of its influence on the photooxidation processes in the retina.
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