Fine Tuning of Canonical and Alternative Functions in Redox Metalloproteins and Metalloenzymes

Title: Fine Tuning of Canonical and Alternative Functions in Redox Metalloproteins and Metalloenzymes

Speaker: Daniel H. Murgida

Affilitation: University of Buenos Aires, CONICET and Eureka Nanobioengineering S.A.

Abstract: Metalloproteins are relatively flexible entities able to sample a broad conformational space, which is a prerequisite to exert charge transfer and catalytic functions. Depending on the specific conditions, interactions, cellular localization, mutations and post-translational modifications, different conformations can be stabilized, which may differ in structure, flexibility, electronic properties, binding affinities, and enzymatic activity. In this seminar I will present some recent examples from our lab showing how the systematic perturbation of these properties allows for an atomistic description of the electron transfer directionality in binuclear CuA centers, dissects the interplay of electron transport and proapoptotic catalytic functions of cytochrome c and enables the design of chimeric mononuclear Cu proteins with novel functionalities. Finally, I will show how, in sharp contrast, the catalytic performance of DyP peroxidases can be drastically improved without the need of structural or physical perturbations by simply actuating the enzyme as a superoxidase.