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FLASH PHOTOLYSIS OF BOVINE SERUM ALBUMIN: IDENTIFICATION AND DECAY KINETICS OF TRANSIENT INTERMEDIATES
Author(s) -
White M.,
Kuntz R. R.,
Ghiron C. A.,
Volkert W. A.
Publication year - 1978
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1978.tb07727.x
Subject(s) - chemistry , indole test , flash photolysis , kinetics , yield (engineering) , adduct , photochemistry , radical , bovine serum albumin , quantum yield , sodium dodecyl sulfate , human serum albumin , serum albumin , triplet state , chromatography , stereochemistry , reaction rate constant , organic chemistry , biochemistry , molecule , fluorescence , physics , materials science , quantum mechanics , metallurgy
. Using the method of flash photolysis, the triplet of the single indole side chain of human serum albumin was detected at room temperature. In a nitrogen saturated solution, this species was found to decay exponentially for over a factor of ten with a lifetime τ 0.5 ms. Analogous experiments, reported here, with bovine serum albumin yield a non‐exponential decay which may be decomposed into two components. The yield of the longer lived triplet, with an average τ of ∼6 ms, is significantly enhanced by addition of a 20 fold excess of sodium dodecyl sulfate or 1 M Br ‐ . The yield of the shorter lived triplet, τ 0.4 ms, is unaffected by these treatments as was previously observed for the single indole in HSA. Thus, the short lived triplet may be assigned to the indole in BSA which is homologous to the one in HSA. The longer lived triplet may be assigned to the remaining indole of BSA. On the bases of wavelength dependence studies, two additional transients may be identified; the electron adduct of the disulfide bond, λ; 420 with a τ 30 ms, and the neutral indole radical,λ; 520 nm with τ ls. These results suggest that the triplet, because of its long τ, will be a valuable intrinsic reporter group for the study of the structure and dynamics of proteins in solution at room temperature.