Femtosecond Dynamics of a Porphyrin Derivative Confined by the Human Serum Albumin Protein

被引:8
作者
Synak, Anna
Ziolek, Marcin
Angel Organero, Juan
Douhal, Abderrazzak [1 ]
机构
[1] Univ Castilla La Mancha, Dept Quim Fis, Fac Ciencias Ambientales & Bioquim, Toledo 45071, Spain
关键词
ULTRAFAST RELAXATION; ABSORPTION; FLUORESCENCE; SPECTROSCOPY; BINDING; ENERGY; PHASE; ZINC;
D O I
10.1021/jp105351h
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The relaxation dynamics of 5,10,15,20-tetrakis(4-hydroxyphenyl)-porphyrin (p-THPP) in tetrahydrofuran (THF) and encapsulated within the human serum albumin (HSA) protein in water solution was investigated. The protein environment affects the B -> Q(y). and Q(x)-> Q(y) transition dynamics (from 80 and 140-200 fs in THF to 50 and 100 fs in HSA, respectively) as well as the lifetime of the relaxed Q. state (9.1 vs 9.9 ns). The most prominent differences are observed in the relaxation dynamics in the hot Q(x) state in HSA, which includes the energy transfer to the protein in similar to 1 ps and much slower solvent-assisted thermal equilibration component of about 20-30 ps.
引用
收藏
页码:16567 / 16573
页数:7
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