Fractal aggregation of porcine fumarase induced by free radicals.
The present study demonstrates that H(2)O(2) and OH(.-) cause fibril aggregation and catalytic inactivation of porcine fumarase. In the aggregated (oxidized) enzyme, modifications in both secondary and tertiary protein structure occur and the enzyme aggregation obeys to fractal geometry. We then collected information on the fractal dimension and on the size and shape of fumarase aggregates by using Synchrotron Radiation (SR) Small Angle X-ray Scattering (SAXS) analysis. The geometrical self-similarity assessment of aggregates has been revealed by both AFM and SEM measurements at different scale of magnification. Micrographs collected remarkably demonstrate that the oxidized enzyme shows dendritic fractal structure over a large range of sizes.
Barteri
Mario
M
Department of Chemistry, University of Rome "La Sapienza", Piazzale Aldo Moro 5, 00185 Rome, Italy. mario.barteri@uniroma1.it
Coluzza
Carlo
C
Rotella
Simona
S
D000818:Animals; D017709:Fractals; D005609:Free Radicals; D005649:Fumarate Hydratase / Q000737:chemistry* / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D012542:Scattering, Radiation; D013552:Swine
D005609:Free Radicals; D005649:Fumarate Hydratase