Fluorescence of luciferases from Luciola mingrelica (single tryptophanresidue, Trp-419) and Photinus pyralis (two tryptophan residues, Trp-417,Trp-426) was studied. Analysis of quenching of tryptophan fluorescenceshowed that the tryptophan residue conserved in all luciferases is notaccessible for charged quenchers, which is explained by the presence ofpositively and negatively charged amino acid residues in the close vicinityto it. An effective energy transfer from tryptophan to luciferin wasobserved during quenching of tryptophan fluorescence of both luciferaseswith luciferin. From the data on the energy transfer, the distance betweenthe luciferin molecule and Trp-417 (419) in the luciferin–luciferasecomplex was calculated: 11–15 Å for P. pyralis and 12–17Å for L. mingrelica luciferases. The role of the conserved Trp residuein the catalysis is discussed.
Fluorescent Properties of Firefly Luciferases and Their Complexes with Luciferin
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
Ekaterina I. Dementieva, Elena A. Fedorchuk, Lubov Yu. Brovko, Alexander P. Savitskii, Natalya N. Ugarova; Fluorescent Properties of Firefly Luciferases and Their Complexes with Luciferin. Biosci Rep 1 February 2000; 20 (1): 21–30. doi: https://doi.org/10.1023/A:1005579016387
Download citation file: