title: Fractal aggregation of porcine fumarase induced by free radicals.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Rome "La Sapienza", Piazzale Aldo Moro 5, 00185 Rome, Italy. mario.barteri@uniroma1.it
authors.forename: Mario
authors.initials: M
authors.lastname: Barteri
authors.forename: Carlo
authors.initials: C
authors.lastname: Coluzza
authors.forename: Simona
authors.initials: S
authors.lastname: Rotella
mesh_terms: D000818:Animals; D017709:Fractals; D005609:Free Radicals; D005649:Fumarate Hydratase / Q000737:chemistry* / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D012542:Scattering, Radiation; D013552:Swine
chemical_list: D005609:Free Radicals; D005649:Fumarate Hydratase