Wednesday, March 21, 2007
Iron Man: ACS Honors Chemistry Professor Eckard Münck
Eckard Münck, professor of chemistry, has received the 2007 Alfred Bader Award, the highest award in bioinorganic and bioorganic chemistry given by the American Chemical Society (ACS). Münck will receive the award at ACS’s National Meeting later this month in Chicago.
The Alfred Bader Award recognizes Münck’s exceptional work on the biophysical properties of metalloproteins, which include iron-based enzymes that catalyze reactions essential to life. Münck’s research has established Mössbauer spectroscopy as a potent tool for studying proteins that contain complex iron centers.
“Eckard is part of an elite group of chemists in the Department of Chemistry at Carnegie Mellon who conduct research in bioinorganic chemistry to understand iron-containing complexes and their relevance to biological processes, environmental remediation and materials science,” said Hyung Kim, professor and head of the department of chemistry.
“Eckard has made seminal contributions to our understanding of the role of metal ions in biology through his powerful application of physical methods, chiefly Mössbauer spectroscopy, for which he is the acknowledged worldwide leader,” said Stephen J. Lippard, Arthur Amos Noyes Professor of Chemistry at the Massachusetts Institute of Technology.
Münck’s talk, “Observing molecules from the inside out(ward): Mössbauer spectroscopy,” will describe how Mössbauer spectroscopy provides a unique advantage over other tools for understanding the function of metal-containing enzymes and proteins at an atomic level.
“By means of brilliant applications of the Mössbauer effect and related theoretical developments in electronic structure, Eckard has revolutionized the study of iron proteins and enzymes. His work is a tour de force in biophysical chemistry,” said Richard H. Holm, Higgins Professor of Chemistry at Harvard University.
“Mössbauer studies of iron proteins by Eckard are the functional equivalents of portraits painted by Leonardo da Vinci,” said Terry Collins, a scientific collaborator and the Thomas Lord Professor of Chemistry and director of the Institute for Green Oxidation Chemistry at Carnegie Mellon.
To honor Münck, the ACS is also holding a symposium that will feature 17 talks by leaders in the field of bioinorganic and bioorganic chemistry. Several Carnegie Mellon faculty members in the Department of Chemistry will be presenting, including Catalina Achim, Emile Bominaar, Collins and Michael Hendrich. The symposium brings together an impressive group of chemists whose innovative work places them at the leading edge of the field of bioinorganic and bioorganic chemistry, according to Achim, assistant professor of chemistry and organizer of the symposium.
Faculty from the Department of Chemistry will each present research related to their studies of complexes containing iron (Fe), the most common metal used in the body. For example, iron helps to carry out many cell functions, and iron complexes help to transport oxygen in the blood and tissues.
Achim will report on Fe(II) complexes that can change magnetic and optical properties in response to changes in temperature. This research is important to understand and rationally design materials with better information storage capacity and transport efficiency.
Bominaar, associate research professor, will discuss his lab’s recent findings using Mössbauer spectroscopy and density functional theory (DFT) calculations to study the electronic structures of a number of high-valent iron complexes, which mimic the properties of active sites present in enzymes in oxidation states essential for oxygen activation.
Collins will discuss features of Fe-TAML activators, catalysts created in his lab that work in combination with oxygen and hydrogen peroxide to convert harmful pollutants into harmless or less toxic substances.
Hendrich, associate professor of chemistry, will present his recent research that identified a unique interaction between several hemes (iron-containing molecules) in the cytochrome b6f complex that is critical to photosynthesis, the process plants use to convert light energy to chemical energy. He will discuss how he used Electron Paramagnetic Resonance (EPR) spectroscopy — a technique that detects molecules that have unpaired electrons — to correlate the function and structure of heme cn in the cytochrome b6f complex.
For more information about bioinorganic chemistry at the Mellon College of Science, please visit:
By: Amy Pavlak