With this award from the Major Research Instrumentation (MRI) Program, Professor Michael Hendrich from Carnegie-Mellon University will acquire an X-band electron paramagnetic resonance (EPR) spectrometer. The award will enhance research training and education at all levels, especially in areas such as (a) metal containing proteins, enzymes, and biomimetic complexes, (b) Mossbauer spectroscopy, EPR and density functional theory calculations of oxygen activating enzymes and biomimetic complexes, (c) control of metals and spin state transitions with nucleic acid duplexes and molecular complexes, (d) probing the electronic structure of quantum-sized metal nanoclusters, (e) studies of artificial water oxidation catalysts, (f) characterization of Fe(III)-tetraanionic tetra-amidomacrocyclic-ligands, (g) cobalt complexes as potential cyanide decorporating agents, (h) molybdenum enzymes and biomimetic complexes, and (i) study of a rare earth crystalline thermometer for EPR spectroscopy.

An EPR spectrometer yields detailed information on the geometric and electronic structure of molecular and solid state materials. It may also be used to obtain information about the lifetimes of free radicals, short-lived, highly reactive species involved in valuable chemical transformations as well as the initiation of pathological tumor growth. These studies will impact a number of areas, from the synthesis of inorganic and organic molecules to the development of new solid state materials to compounds of biological interest. Employing examples inspired from ongoing research, this instrument will be an integral part of research and teaching at the undergraduate and graduate levels at Carnegie-Mellon University as well as at the University of Pittsburgh, Duquesne University and Allegheny College.

Project Report

Proteins and enzymes containing transition metals are essential for a wide range of basic processes of life, including DNA synthesis, metabolism, photosynthesis, detoxification. Synthetic complexes containing transition metals that mimic the catalytic chemistry of enzymes, but without the delicate protein, are important for chemical and energy transformations. Electron Paramagnetic Resonance (EPR) spectroscopy has long been a primary method for molecular level characterization of metal centers in materials and biological complexes. Carnegie Mellon University, University of Pittsburgh Duquesne University, and Allegheny College have strong groups of researcher and educators in scientific areas involving synthetic and biological metal complexes. This award provided finds for the purchase of a new EPR spectrometer which replaced an instrument that had been maintained for over 24 years of service to researchers in western Pennsylvania. EPR spectroscopy is critical research instrumentation which is essential to the infrastructure of Chemistry departments. Multiple research groups from the schools listed above regularly use the instrument. The new EPR spectrometer became operational in February 2013. Over the years, the study of many different types of metals in synthetic complexes and proteins in our laboratories have led to a development of a systematic methodology for the quantitative interpretation of EPR spectra. We offer assistance to external users who need help in spectral acquisition and interpretation.

National Science Foundation (NSF)
Division of Chemistry (CHE)
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Carlos A. Murillo
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Carnegie-Mellon University
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