Hendrich Builds Tools as Well as Knowledge
Heidi Opdyke
- Associate Dean of Marketing and Communications, MCS
- Email opdyke@andrew.cmu.edu
- Phone 412-268-9982
Michael Hendrich spent his career pushing the limits of magnetic resonance spectroscopy. Over 32 years at Carnegie Mellon, the chemistry professor transformed how scientists study metalloproteins, developing both the instruments and the analytical tools needed to probe the metal centers that drive life’s essential reactions.
Roughly one-third of proteins in the human body contain metals, including enzymes that are indispensable to nearly all forms of life. These metalloenzymes power processes ranging from energy conversion and DNA replication to detoxification and oxygen transport. But studying the transition metals at their core is notoriously difficult. Traditional biochemical methods often fall short. Hendrich built his career tackling that challenge.
Early on, he pioneered the use of parallel-mode electron paramagnetic resonance (EPR), a variation that aligns the oscillating magnetic field parallel to the applied field. Used alongside conventional (transverse mode) EPR, the technique allows researchers to detect metal centers with both odd and even numbers of unpaired electrons, broadening what scientists can observe. His expertise extended across complementary methods, including Mössbauer spectroscopy and SQUID magnetometry, which together allow scientists to characterize metalloproteins at the atomic level.
But Hendrich didn’t stop at instrumentation. He also built the computational tools needed to interpret complex data, developing a custom software package, SpinCount, to simulate spectroscopic signals. The combination of experiment and computation helped establish quantitative EPR as a powerful approach for studying metal-containing enzymes.
Using this broad approach, Hendrich has contributed to a greater understanding of multiple biochemical systems, including multiheme proteins involved in electron transport, manganese-dependent oxygenases, biological iron-sulfur clusters, and both heme and non-heme iron enzymes. He identified and characterized reactive intermediates — short-lived states that form as enzymes carry out chemical reactions. By spectroscopically characterizing these intermediates, scientists can identify chemical steps involved in an enzymatic transformation.
Hendrich also worked closely with synthetic chemists, studying model metal complexes designed to mimic enzyme function. These collaborations connected carefully controlled laboratory systems with complex biological ones, helping validate proposed reaction pathways.
His career stands out for its breadth. Hendrich moved fluidly between spectroscopy, instrument design, computation, and biochemistry. As he retires, his work continues to drive the field forward — from the discoveries he made to the tools, methods and ways of thinking he helped build, leaving researchers better equipped to take the next steps.
Alongside his research, Hendrich maintained a strong commitment to teaching and mentorship. He guided undergraduate, graduate and postdoctoral researchers, many of whom have gone on to establish their own careers. And he taught a wide range of courses, from physical chemistry, math for chemists and physical chemistry laboratory for undergraduates, to graduate-level physical inorganic chemistry. In the classroom, he was known for making complex ideas accessible, using simple, memorable demonstrations — such as rope tricks to illustrate eigenfunctions — to bring abstract concepts to life.
