Metal Clusters and DAFS: A Comprehensive Analysis of Electronic Structure and Reactivity

In nature, small molecule activations are executed by multinuclear transition metal clusters embedded within the protein superstructures of enzymes. The close positioning of the metal centers enables them to collaborate in substrate binding and facilitate multielectron redox processes. To gain a more profound understanding of the fundamental relationships between structure and properties governing the behavior of individual metal atoms within clusters, obtaining metal site-specific information becomes crucial. One emerging method to achieve this knowledge is resonant diffraction anomalous fine structure (DAFS), which allows for the investigation of homometallic clusters on a metal site-specific basis. The focus of this thesis is DAFS analysis on synthetic multi-Cu clusters, which are significant to biomimetic enzymatic sites or to be used in significant chemical transformations such as N2O and CO2 reduction.