Conformational change induced by coenzyme binding to bovine liver dihydrofolate reductase: a spectrofluorimetric study
| Autor: | M. Sarrazin, M. Chauvet, M. Bourdeaux, O. Rimet |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Conformational change
Protein Conformation Stereochemistry Biophysics Fluorescence spectrometry Biochemistry Protein structure Structural Biology parasitic diseases Dihydrofolate reductase Animals Coenzyme binding Molecular Biology Conformational isomerism chemistry.chemical_classification biology Chemistry Kinetics Tetrahydrofolate Dehydrogenase Spectrometry Fluorescence Enzyme Energy Transfer Liver biology.protein NADPH binding Cattle Oxidation-Reduction NADP Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1076:435-438 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(91)90488-l |
| Popis: | When NADPH was added in excess to a bovine liver DHFR solution, a fluorescence peak due to an energy transfer mechanism was apparent at 450 nm. It did not vary over time. The intrinsic fluorescence peak of DHFR at 320 nm was quenched and this phenomenon increased over the time-course after NADPH addition. This result was ascribed to a slow DHFR conformational change induced by NADPH binding, which has never been previously described in such a long time scale (more than 30 min). A kinetic scheme accounting for this mechanism has been proposed. Furthermore, this interconversion between two protein conformers led to an increase in the initial apparent rate of the enzymatic reaction catalyzed by DHFR. |
| Databáze: | OpenAIRE |
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