Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537083 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2009 | 6 Pages |
Abstract
α-Synuclein, the pathological component of Parkinson's disease, has been demonstrated to be highly interactive with various protein partners. α-Synuclein has been shown to exert a novel effect on the bioluminescence of firefly luciferase by stimulating the oxyluciferin formation from its substrate of luciferin, which results in a significant enhancement of the spike of flashing light via concomitant augmentation for both rapid rise and quick decay of the luminescence. Binding affinity between α-synuclein and luciferase was evaluated with Kd of 8.1 µM based on a dose-dependent enhancement of the luciferase activity by α-synuclein. Kinetic analyses indicated that α-synuclein has facilitated luciferin localization to the luciferase by decreasing apparent Km, which makes the maximum rate of bioluminescence no longer dependent upon ATP concentration. Catalytic consequences of the α-synuclein binding to luciferase have led to a delayed onset of the coenzyme A-mediated retardation of the quick decay of flashing light as well as a shift in the emission spectra of bioluminescence. Taken together, the novel effects of α-synuclein toward the bioluminescence of luciferase have been demonstrated to be initiated by the specific molecular interaction between the proteins which has influenced the substrate (luciferin) localization to the enzyme.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Jehoon Kim, Chung Hee Moon, Seunho Jung, Seung R. Paik,