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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2937
Título : | Unraveling the mechanisms of tryptophan fluorescence quenching in the triosephosphate isomerase from Giardia lamblia |
Creador: | Hernández Alcántara, Gloria |
Nivel de acceso: | Open access |
Palabras clave : | Giardia lamblia - enzimología Triosa-Fosfato Isomerasa - química Triptófano - metabolismo Giardia lamblia - enzymology Triose-Phosphate Isomerase - chemistry Tryptophan - metabolism Giardia Triosephosphate isomerase Glicólisis Interacción aromática Espectroscopia Enfriamiento Ambiente de triptófano Giardia Triosephosphate isomerase Glycolysis Aromatic interaction Spectroscopy Quenching Tryptophan environment |
Descripción : | In the native state several proteins exhibit a quenching of fluorescence of their tryptophans. We studied triosephosphate isomerase from Giardia lamblia (GlTIM) to dissect the mechanisms that account for the quenching of fluorescence of its Trp. GlTIM contains four Trp per monomer (Trp75, Trp162, Trp173, and Trp196) distributed throughout the 3D structure. The fluorescence of the denatured enzyme is 3-fold higher than that of native GlTIM. To ascertain the origin of this phenomenon, single and triple mutants of Trp per Phe were made. The intrinsic fluorescence was determined, and the data were interpreted on the basis of the crystal structure of the enzyme. Our data show that the fluorescence of all Trp residues is quenched through two different mechanisms. In one, fluorescence is quenched by aromatic-aromatic interactions due to the proximity and orientation of the indole groups of Trp196 and Trp162. The magnitude of the quenching of fluorescence in Trp162 is higher than in the other three Trp. Fluorescence quenching is also due to energy transfer to the charged residues that surround Trp 75, 173 and 196. Further analysis of the fluorescence of GlTIM showed that, among TIMs from other parasites, Trp at position 12 exhibits rather unique properties. © 2008. |
Colaborador(es) u otros Autores: | Rodríguez-Romero A Reyes-Vivas H Peon J Cabrera N Ortiz C Enríquez-Flores S De la Mora-De la Mora I López-Velázquez G |
Fecha de publicación : | 2008 |
Tipo de publicación: | Artículo |
Formato: | |
Identificador del Recurso : | 10.1016/j.bbapap.2008.05.016 |
Fuente: | Biochimica et Biophysica Acta - Proteins and Proteomics 1784(11):1493 - 1500 |
URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2937 |
Idioma: | eng |
Aparece en las colecciones: | Artículos |
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