Enantioselective Quenching of Room-Temperature Phosphorescence Lifetimes of Proteins: Bovine and Human Serum Albumins
- 3 February 2007
- journal article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 8 (3), 761-764
- https://doi.org/10.1021/bm0610121
Abstract
Enantioselective quenching of the room-temperature phosphorescence (RTP) lifetime of proteins was demonstrated due to the effects of various external chiral quenching agents. In the absence of quenchers, the RTP lifetimes for bovine serum albumin (BSA) and human serum albumin (HSA) were found to be 5.0 +/- 0.2 and 4.0 +/- 0.1 ms, respectively. The addition of various chiral quenchers (three pairs of binaphthols and two pairs of beta-blockers) into the deoxygenated sample solutions containing BSA and HSA reduced their RTP lifetimes significantly, i.e., from ca. 4-5 ms (in the absence) to an average lifetime of ca. 1-2 ms (in the presence) of the chiral quenchers. For the R and S enantiomers examined, marked differences in RTP lifetimes were observed, i.e., ranging from ca. 20-29% for the binaphthols to ca.14-16% for the beta-blockers. Such findings could lead to a better understanding of the relationship between chirality, dynamics/conformational changes, and biological functions of proteins.Keywords
This publication has 27 references indexed in Scilit:
- Substrate-induced Conformational Changes in the Membrane-embedded IICmtl-domain of the Mannitol Permease from Escherichia coli, EnzymeIImtl, Probed by Tryptophan Phosphorescence SpectroscopyPublished by Elsevier ,2005
- Large chiral discrimination of a molecular probe by bovine serum albuminChemical Communications, 2001
- Pressure−Temperature Effects on Oxygen Quenching of Protein PhosphorescenceJournal of the American Chemical Society, 1999
- Comparison of the Time‐resolved Absorption and Phosphorescence from the Tryptophan Triplet State in Proteins in SolutionPhotochemistry and Photobiology, 1998
- Conformational changes in proteins induced by dynamic associations. A tryptophan phosphorescence studyEuropean Journal of Biochemistry, 1994
- Excited triplet states as probes in organized systems. An overview of recent resultsJournal of Photochemistry and Photobiology A: Chemistry, 1992
- Quenching of tryptophan phosphorescence in Escherichia coli alkaline phosphatase by long-range transfer mechanisms to external agents in the rapid-diffusion limitBiochemistry, 1991
- Tryptophan luminescence from liver alcohol dehydrogenase in its complexes with coenzyme. A comparative study of protein conformation in solutionBiochemistry, 1990
- THE TRIPLET STATE AS A PROBE OF DYNAMICS AND STRUCTURE IN BIOLOGICAL MACROMOLECULESPhotochemistry and Photobiology, 1989
- TRYPTOPHAN PHOSPHORESCENCE AT ROOM TEMPERATURE AS A TOOL TO STUDY PROTEIN STRUCTURE AND DYNAMICSPhotochemistry and Photobiology, 1989