Thomas Spatzal

2.3k total citations · 1 hit paper
26 papers, 1.9k citations indexed

About

Thomas Spatzal is a scholar working on Renewable Energy, Sustainability and the Environment, Inorganic Chemistry and Catalysis. According to data from OpenAlex, Thomas Spatzal has authored 26 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Renewable Energy, Sustainability and the Environment, 14 papers in Inorganic Chemistry and 7 papers in Catalysis. Recurrent topics in Thomas Spatzal's work include Metalloenzymes and iron-sulfur proteins (22 papers), Metal-Catalyzed Oxygenation Mechanisms (12 papers) and Electrocatalysts for Energy Conversion (11 papers). Thomas Spatzal is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (22 papers), Metal-Catalyzed Oxygenation Mechanisms (12 papers) and Electrocatalysts for Energy Conversion (11 papers). Thomas Spatzal collaborates with scholars based in United States, Germany and France. Thomas Spatzal's co-authors include Douglas C. Rees, Oliver Einsle, Susana L. A. Andrade, Kathryn Perez, Limei Zhang, James B. Howard, Stefan Weber, Erik Schleicher, Julia Schlesier and Daniel Sippel and has published in prestigious journals such as Science, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Thomas Spatzal

26 papers receiving 1.9k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

2011 728 citations Thomas Spatzal, Limei Zhang et al. Science profile →

Peers

Countries citing papers authored by Thomas Spatzal

Since Specialization

Citations

This map shows the geographic impact of Thomas Spatzal's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Thomas Spatzal with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Thomas Spatzal more than expected).

Fields of papers citing papers by Thomas Spatzal

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas Spatzal. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Thomas Spatzal. The network helps show where Thomas Spatzal may publish in the future.

Co-authorship network of co-authors of Thomas Spatzal

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas Spatzal. A scholar is included among the top collaborators of Thomas Spatzal based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Thomas Spatzal. Thomas Spatzal is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

#	Work	Indexed citations
1	Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra 2024 ·Nature Communications ·(unknown), Kathryn Perez, Thomas Spatzal, Oliver Einsle, Stefan Weber, Douglas C. Rees, (unknown)	1
2	Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins 2024 ·Nature Protocols ·(unknown), (unknown), Thomas Spatzal, Douglas C. Rees	6
3	Mechanism of molybdate insertion into pterin-based molybdenum cofactors 2021 ·Nature Chemistry ·(unknown), Jing Yang, J. Krausze, (unknown), Casseday P. Richers, Thomas Spatzal, (unknown), Logan J. Giles, Douglas C. Rees, Ralf R. Mendel, Martin L. Kirk, Tobias Kruse	27
4	Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site 2020 ·Angewandte Chemie International Edition ·Trixia M. Buscagan, Kathryn Perez, Ailiena O. Maggiolo, Douglas C. Rees, Thomas Spatzal	59
5	Site‐Specific Oxidation State Assignments of the Iron Atoms in the [4Fe:4S]^2+/1+/0 States of the Nitrogenase Fe‐Protein 2019 ·Angewandte Chemie ·(unknown), Thomas Spatzal, Douglas C. Rees	1
6	Site‐Specific Oxidation State Assignments of the Iron Atoms in the [4Fe:4S]^2+/1+/0 States of the Nitrogenase Fe‐Protein 2019 ·Angewandte Chemie International Edition ·(unknown), Thomas Spatzal, Douglas C. Rees	36
7	Reversible Protonated Resting State of the Nitrogenase Active Site 2017 ·Journal of the American Chemical Society ·Christine N. Morrison, Thomas Spatzal, Douglas C. Rees	31
8	Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement 2016 ·Nature Communications ·Thomas Spatzal, Julia Schlesier, (unknown), Daniel Sippel, Limei Zhang, Susana L. A. Andrade, Douglas C. Rees, Oliver Einsle	133
9	Production and isolation of vanadium nitrogenase from Azotobacter vinelandii by molybdenum depletion 2016 ·JBIC Journal of Biological Inorganic Chemistry ·Daniel Sippel, Julia Schlesier, Michael F. Rohde, Christian Trncik, Laure Decamps, Ivana Djurdjević, Thomas Spatzal, Susana L. A. Andrade, Oliver Einsle	34
10	Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor 2015 ·eLife ·Thomas Spatzal, Kathryn Perez, James B. Howard, Douglas C. Rees	120
11	Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase 2014 ·Science ·Thomas Spatzal, Kathryn Perez, Oliver Einsle, James B. Howard, Douglas C. Rees	343
12	The Center of Biological Nitrogen Fixation: FeMo‐Cofactor 2014 ·Zeitschrift für anorganische und allgemeine Chemie ·Thomas Spatzal	14
13	Structural and functional characterization of 4-hydroxyphenylpyruvate dioxygenase from the thermoacidophilic archaeon Picrophilus torridus 2014 ·Extremophiles ·(unknown), Thomas Spatzal, S. Gerhardt, Andreas Krämer, Oliver Einsle, Wolfgang Hüttel	2
14	Identification of a spin-coupled Mo(iii) in the nitrogenase iron–molybdenum cofactor 2014 ·Chemical Science ·Ragnar Björnsson, Frederico A. Lima, Thomas Spatzal, Thomas Weyhermüller, Pieter Glatzel, Eckhard Bill, Oliver Einsle, Frank Neese, Serena DeBeer	156
15	The Sixteenth Iron in the Nitrogenase MoFe Protein 2013 ·Angewandte Chemie International Edition ·Limei Zhang, Jens T. Kaiser, Gabriele Meloni, (unknown), Thomas Spatzal, Susana L. A. Andrade, Oliver Einsle, James B. Howard, Douglas C. Rees	31
16	Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single‐Crystal EPR Spectroscopy 2013 ·Angewandte Chemie International Edition ·Thomas Spatzal, Oliver Einsle, Susana L. A. Andrade	22
17	The Sixteenth Iron in the Nitrogenase MoFe Protein 2013 ·Angewandte Chemie ·Limei Zhang, Jens T. Kaiser, Gabriele Meloni, (unknown), Thomas Spatzal, Susana L. A. Andrade, Oliver Einsle, James B. Howard, Douglas C. Rees	5
18	Turnover-Dependent Inactivation of the Nitrogenase MoFe-Protein at High pH 2013 ·Biochemistry ·(unknown), Chad Haynes, Thomas Spatzal, Douglas C. Rees, James B. Howard	26
19	MacA is a Second Cytochrome c Peroxidase of Geobacter sulfurreducens 2012 ·Biochemistry ·(unknown), (unknown), (unknown), (unknown), Thomas Spatzal, S. Gerhardt, Sean J. Elliott, Oliver Einsle	37
20	Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I) 2010 ·Biochimica et Biophysica Acta (BBA) - Bioenergetics ·Thomas Pohl, Thomas Spatzal, (unknown), Erik Schleicher, Arpad Mihai Rostas, (unknown), (unknown), Corinne Boudon, Petra Hellwig, Stefan Weber, Thorsten Friedrich	12

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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