Thomas Spatzal
| Thomas Spatzal | |
|---|---|
| Born | 1983 |
| 🏳️ Nationality | German |
| 💼 Occupation | |
Thomas Spatzal is a German biochemist and biophysicist known for his work in structural biology.[1] He has made various contributions to the understanding of complex metal-containing proteins, particularly in the field of biological nitrogen fixation.
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.[2] He made contributions to the understanding of nitrogenase, one of nature's most complex protein systems.[3][4]
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.[5] His research has provided insights into biological dinitrogen reduction,[4] as well as carbon-carbon coupling reactions,[6][7] which have implications for the development of sustainable energy sources and environmental protection.[5]
Parts of his research led to the conclusive structural characterization of FeMoco, the active site of nitrogenase,[8] evidence for substrate binding to the active site,[6] and evidence for major structural rearrangements of the catalytic center during turnover.[9] His work has changed the understanding of the mode-of-action of biological nitrogen reduction, and contributed to the structure-based investigation of the enzyme's catalytic mechanism.[8][10] His research based on X-ray crystallography has helped to shed light on some of nature's most complex processes.
References
- ↑ "Thomas Spatzal / Research Profile".
- ↑ "Rees Group".
- ↑ "Figuring out how we get the nitrogen we need".
- ↑ 4.0 4.1 Spatzal, Thomas; Aksoyoglu, Müge; Zhang, Limei; Andrade, Susana L. A.; Schleicher, Erik; Weber, Stefan; Rees, Douglas C.; Einsle, Oliver (2011-11-18). "Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor". Science. 334 (6058): 940. Bibcode:2011Sci...334..940S. doi:10.1126/science.1214025. ISSN 0036-8075. PMC 3268367. PMID 22096190.
- ↑ 5.0 5.1 "Researchers elucidate how a nitrogen-fixing enzyme also produces hydrocarbons".
- ↑ 6.0 6.1 Spatzal, Thomas; Perez, Kathryn A.; Einsle, Oliver; Howard, James B.; Rees, Douglas C. (2014-09-26). "Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase". Science. 345 (6204): 1620–1623. Bibcode:2014Sci...345.1620S. doi:10.1126/science.1256679. ISSN 0036-8075. PMC 4205161. PMID 25258081.
- ↑ Buscagan, Trixia M.; Perez, Kathryn A.; Maggiolo, Ailiena O.; Rees, Douglas C.; Spatzal, Thomas (2021-01-27). "Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site". Angewandte Chemie International Edition. 60 (11): 5704–5707. doi:10.1002/anie.202015751. ISSN 1433-7851. PMC 7920927 Check
|pmc=value (help). PMID 33320413 Check|pmid=value (help). - ↑ 8.0 8.1 Ramaswamy, S. (2011-11-18). "One Atom Makes All the Difference". Science. 334 (6058): 914–915. Bibcode:2011Sci...334..914R. doi:10.1126/science.1215283. ISSN 0036-8075. PMID 22096179. Unknown parameter
|s2cid=ignored (help) - ↑ Chen, Percival Yang-Ting; Wittenborn, Elizabeth C; Drennan, Catherine L (2016-02-03). "Waltzing around cofactors". eLife. 5: e13977. doi:10.7554/elife.13977. ISSN 2050-084X. PMC 4758945. PMID 26843316. Unknown parameter
|s2cid=ignored (help) - ↑ Högbom, Martin (2014-09-26). "A dynamic tool for nitrogen reduction". Science. 345 (6204): 1568. Bibcode:2014Sci...345.1568H. doi:10.1126/science.1260021. ISSN 0036-8075. PMID 25258069. Unknown parameter
|s2cid=ignored (help)
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