Thomas Spatzal is a German biochemist and biophysicist known for his work in structural biology. He has made various contributions to the understanding of complex metal-containing proteins, particularly in the field of biological nitrogen fixation.
Early life and education
Spatzal was born and raised in Baden-Wuerttemberg, Germany. He received his early education in the region before going on to study at the Albert-Ludwigs-University Freiburg, where he obtained a M.Sc. degree in chemistry in 2008. In 2012 he received a PhD in biochemistry from the same institution.
Career
Following his PhD, Spatzal joined the laboratory of Douglas C. Rees as a postdoctoral scholar and as a Howard Hughes Medical Institute fellow at the California Institute of Technology in Pasadena, CA. He made notable contributions to the understanding of nitrogenase, one of nature's most complex protein systems.
Since 2016, Spatzal has held several positions in the biopharmaceutical industry, including a role as Senior Director for Analytical R&D as of 2022. Despite his focus on industrial research, he has remained active in academic research as an Associate Guest researcher and Lecturer at the California Institute of Technology from 2016 to 2023.
Research
Spatzal's research activities are focused on the structure and function of complex metal-containing proteins with a special emphasis on biological nitrogen fixation. His work on nitrogenase has led to insights into how nature accomplishes Haber-Bosch- and Fischer-Tropsch- type chemistry. His research has provided key insights into biological dinitrogen reduction, as well as carbon-carbon coupling reactions, which have implications for the development of sustainable energy sources and environmental protection.
Spatzal's research in the area of nitrogen fixation pioneered the detailed structure-guided characterization of the enzyme's catalytic mechanism. Parts of his research led to the first conclusive structural characterization of the active site of nitrogenase (FeMoco), evidence for substrate binding to the active site, and evidence for key structural rearrangements of the catalytic center during turnover. His work has redefined the understanding of the mode of action of biological nitrogen reduction, and marked a paradigm shift for the structure-based investigation of the enzyme's catalytic mechanism. His research based on X-ray crystallography has helped to shed light on some of nature's most complex processes.