Friday, April 14th
106 Stanley Hall
Speaker 1: Adam M. Perez (Jeremy Thorner lab)
The role of the septin cytoskeleton in the control of the yeast cell cycle
Septins are a conserved family of Eukaryotic cytoskeletal elements. These proteins are small GTPases that self-polymerize into heteromeric rods, which serve as the base building units of diverse septin super-structures. In the cell, septin architectures play essential roles in many biological processes, including cytokinesis, membrane remodeling, morphogenesis, and cell-cycle regulation. Septins accomplish these feats in part by serving as a scaffold that recruits a host of downstream effectors to sub-cellular sites in response to upstream inputs. In the budding yeast Saccharomyces cerevisiae
Speaker 2: Raúl H. Lavorie (T. Don Tilley lab)
Artificial metalloproteins with Co4(µ3-O)4 cubanes as active sites. Towards a molecular and electronic control using a protein as a host.
The biological energy intake in photosynthetic systems involves a distorted Mn4O5Ca cubane as active site for the water oxidation reaction. Whereas, synthetic systems that perform this reaction are metal oxides that feature cubane oxo structural motives. In this context, Co4(µ3-O)4 cubanes are used as molecular models of cobalt oxide for the oxygen evolution reaction (OER). These platforms are possible to substitute with different ligands in order modify its redox behavior or attach tailoring motives. This work presents the efforts to use a proteic environment to tune the reactivity of a molecular OER catalyst using the biotin-streptavidin technology