Grinnell College recently issued the following announcement.
Danforth Lecture Series
Sponsored by the Chemistry Department
Dr. Andy Borovik
Distinguished Professor
Department of Chemistry
University of California - Irvine
Public Talk
Wednesday, February 23rd, 2022
Noon
HSSC Multipurpose Room A1231
Putting Atoms in their Place One Bond at a Time
Architects design buildings relying on the proper placement of key materials such as bricks and mortar during construction. Molecular architects design molecules following similar guidelines in that the precise placement of atoms, ions, and bonds is needed to ensure the correct chemical action. Molecular science is driven by the development of new molecules but coming up with original designs is arguably one of the most challenging tasks for scientists. One source of inspiration are natural molecules such as proteins whose structures can provide clues for how to design new compounds. The relationships between biological and abiotic molecules are apparent in the chemistry that powers our plant. There are numerous proteins that react with common and abundant molecules on Earth that include N2, O2, CO2, H2, and water to produce resources that are essential for life. In nature, these reactions are catalyzed by proteins which contain metal ions at their "active sites" that is, the sites in the proteins where chemical reactions occur. There are growing efforts to duplicate the structures of these active sites in artificial molecules to develop more substantiable systems. Successful duplication would have large payoffs with environmental and economic benefits to help our planet.
Chemistry Department Talk
Thursday, February 24, 2022
Noon
HSSC S3325
Lessons from Nature: Incorporating Molecular Complexity within Metal Complexes
Location matters…no compound operates in isolation without interacting with its local environment. Metalloproteins are example systems whose active sites contain intricate structures that aid the performance of specific functions with high selectivities and efficiencies. The complexity of these systems complicates the study of their function and the understanding of the properties that give rise to their reactivity. One approach that has contributed to the current level of knowledge is the study of synthetic constructs that mimic one or more aspects of the native metalloproteins. These systems allow for analysis of individual components of structure and how they affect function. We are thus able to establish structure-function correlations that are necessary for evaluating mechanisms. Using key architectural features from active sites of metalloproteins as inspiration, my group has developed design approaches to prepare systems that regulate local environments around a metal center. This presentation will highlight our design concepts for developing artificial metalloprotein and how they are used to engineered new mono- and di-Fe sites within protein hosts.
Original source can be found here.
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