The environment of the tryptophan residue in Pseudomonas aeruginosa azurin and its fluorescence properties.
Special analysis of the tryptophan residue localization in the structure of the macromolecule of Pseudomonas aeruginosa azurin made it possible to prove many explanations in the existing literature of the extraordinary fluorescence properties of this protein, to choose between various contradictory conclusions and in some cases even to make new interpretations of the known experimental data. It has been revealed that the microenvironment of the tryptophan residue is in principle formed by non-polar hydrocarbon groups. The density of the microenvironment is not very high and there are cavities around the ring. The conformation of the side chain of the tryptophan residue is unstrained. These results have been analysed in connection with available data on the unique short-wave fluorescence spectrum position and the existence of the high-frequency indole ring mobility with significant amplitude. Judging by the distance between tryptophan and tyrosine residues and their mutual orientation, the conclusion was made that there is no energy transfer from Tyr 72 to tryptophan and that the efficiency of the energy transfer from Tyr 108 to tryptophan is about 0.5. The mechanism of the dramatic increase in fluorescence efficiency when the copper atom is removed has been discussed with due regard to the fact that the 'blue' copper centre is displaced from the indole ring by more than 10 A.
D000595:Amino Acid Sequence; D001400:Azurin; D001426:Bacterial Proteins; D008958:Models, Molecular; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa; D013050:Spectrometry, Fluorescence / Q000379:methods; D014364:Tryptophan
D001426:Bacterial Proteins; D001400:Azurin; D014364:Tryptophan