Studies of phosphorescent probes for proteins.
1. Certain capabilities and limitations of using bound phosphorescent chromophores to study protein structure were investigated. Carbonic anhydrase inhibitors with three different arrangements of singlet and triplet energy levels relative to those of tryptophan were used to determine their ability to transfer triplet energy. 2. Ligands representing each of the three spectroscopic energy level arrangements were found to exhibit triplet-triplet energy transfer with a tryptophan residue at the active site of carbonic anhydrase. This greatly increases the number of ligands which may be useful as phosphorescent probes. 3. The efficiency of energy transfer occurs to varying degrees depending upon the inhibitor. This is a potential source of data for determining the position of the ligand in the binding site.
McCarville
M
M
Department of Chemistry, Western Michigan University, Kalamazoo, Mich. 49001, USA.
Hauxwell
R
R
D000818:Animals; D001665:Binding Sites; D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D002256:Carbonic Anhydrases / Q000097:blood / Q000737:chemistry*; D002417:Cattle; D004735:Energy Transfer; D004912:Erythrocytes / Q000201:enzymology; D005016:Ethoxzolamide / Q000737:chemistry* / Q000494:pharmacology; D008163:Luminescent Measurements; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013449:Sulfonamides / Q000737:chemistry* / Q000494:pharmacology; D014364:Tryptophan
D002257:Carbonic Anhydrase Inhibitors; D011506:Proteins; D013449:Sulfonamides; D014364:Tryptophan; D002256:Carbonic Anhydrases; D005016:Ethoxzolamide