TY - JOUR
T1 - Triplet excited states of polycyclic aromatic compounds as probes of their microenvironment in serum albumin complexes
AU - Geacintov, Nicholas E.
AU - Flamer, Thomas J.
AU - Prusik, Thaddeus
AU - Khosrofian, John M.
N1 - Funding Information:
This investigation was supported by Public Health Service Research Grant CA 14980 from the National Cancer Institute and by a Health Research Council City of New York Grant No. U-2312, Partial assistance from an Atomic Energy Commission grant to the Radiation and Solid State Laboratory is also acknowledged. We are indebted to Professor D.I. Schuster for permission to use his xenon lamp flash photolysis apparatus and to Dr. J.
PY - 1975/6/16
Y1 - 1975/6/16
N2 - Using flash photolysis techniques, the triplet excited states of benzo(a)pyrene, pyrene, benz(a)anthracene and other aromatic hydrocarbons have been detected in complexes of bovine (and human) serum albumin dissolved in aqueous solutions at room temperature. The triplet lifetimes can be adjusted to any value within the microsecond-millisecond time domains by varying the partial pressure of oxygen from zero to one atmosphere, thus providing a useful probe on these time scales. Local oxygen concentrations as low as ∼ 2 × 10-7M can be detected. In air saturated solutions, the triplet lifetimes are sensitive to pH dependent conformational changes of the host bovine serum albumin molecules.
AB - Using flash photolysis techniques, the triplet excited states of benzo(a)pyrene, pyrene, benz(a)anthracene and other aromatic hydrocarbons have been detected in complexes of bovine (and human) serum albumin dissolved in aqueous solutions at room temperature. The triplet lifetimes can be adjusted to any value within the microsecond-millisecond time domains by varying the partial pressure of oxygen from zero to one atmosphere, thus providing a useful probe on these time scales. Local oxygen concentrations as low as ∼ 2 × 10-7M can be detected. In air saturated solutions, the triplet lifetimes are sensitive to pH dependent conformational changes of the host bovine serum albumin molecules.
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U2 - 10.1016/0006-291X(75)90826-8
DO - 10.1016/0006-291X(75)90826-8
M3 - Article
C2 - 49184
AN - SCOPUS:0016784472
VL - 64
SP - 1245
EP - 1252
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -