Study of photoinduced energy and electron transfer in alpha-terthienyl-bovine serum albumin conjugates: A laser flash photolysis study

被引:16
作者
Boch, R
Mohtat, N
Lear, Y
Arnason, JT
Durst, T
Scaiano, JC
机构
[1] UNIV OTTAWA,OTTAWA CARLETON CHEM INST,DEPT CHEM,OTTAWA,ON K1N 6N5,CANADA
[2] UNIV OTTAWA,OTTAWA CARLETON INST BIOL,OTTAWA,ON K1N 6N5,CANADA
[3] UNIV OTTAWA,OTTAWA CARLETON CHEM INST,DEPT BIOL,OTTAWA,ON K1N 6N5,CANADA
关键词
D O I
10.1111/j.1751-1097.1996.tb02426.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The photochemistry of alpha-terthienyl (alpha-T) has been examined in bovine serum albumin (BSA), Freely associated and covalently conjugated alpha-T chromophores show similar behavior toward nonpolar quenchers such as oxygen and benzoquinone but show significant differences in the case of quenching by methyl viologen, a water-soluble cationic electron acceptor; in this case, triplet quenching reveals two distinct alpha-T populations, attributed to chromophores in sites showing very different accessibility from the aqueous phase. Rate constants for triplet quenching in BSA are generally slower than those observed in homogeneous solution for free alpha-T. For example, in the case of oxygen, the rate constant is about one order of magnitude smaller when alpha-T is associated or conjugated with the protein compared with alpha-T in solution. While triplet yields for alpha-T are essentially the same in solution and in the protein environment, the yield of detectable singlet oxygen is substantially reduced in the protein. This is attributed to a geminate reaction within the protein involving singlet oxygen trapping in the vicinity of the generation site.
引用
收藏
页码:92 / 99
页数:8
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