Keith O. Hodgson
About
Keith O. Hodgson is a scholar working on Inorganic Chemistry, Materials Chemistry and Renewable Energy, Sustainability and the Environment.
According to data from OpenAlex, Keith O. Hodgson has authored 418 papers receiving a total of 25.7k indexed citations (citations by other indexed papers that have themselves been cited), including 201 papers in Inorganic Chemistry, 136 papers in Materials Chemistry and 110 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Keith O. Hodgson's work include Metal-Catalyzed Oxygenation Mechanisms (146 papers), Metal complexes synthesis and properties (103 papers) and Metalloenzymes and iron-sulfur proteins (86 papers). Keith O. Hodgson is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (146 papers), Metal complexes synthesis and properties (103 papers) and Metalloenzymes and iron-sulfur proteins (86 papers). Keith O. Hodgson collaborates with scholars based in United States, Japan and Italy. Keith O. Hodgson's co-authors include Britt Hedman, Edward I. Solomon, James E. Penner‐Hahn, Sebastian Doniach, T. Daniel P. Stack, Tami E. Westre, Patrick Frank, Jane G. DeWitt, Pierre Kennepohl and R. H. Holm and has published in prestigious journals such as Nature, Science and Chemical Reviews.
In The Last Decade
Keith O. Hodgson
415 papers receiving 24.9k citations
Hit Papers
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Keith O. Hodgson United States | 83 | 10.1k | 8.5k | 5.6k | 5.5k | 4.5k | 418 | 25.7k | ||
| Britt Hedman United States | 71 | 7.9k 0.8× | 5.8k 0.7× | 4.3k 0.8× | 3.3k 0.6× | 3.6k 0.8× | 301 | 17.4k | ||
| Serena DeBeer Germany | 67 | 6.3k 0.6× | 4.8k 0.6× | 4.7k 0.8× | 1.7k 0.3× | 2.6k 0.6× | 312 | 15.0k | ||
| Per E. M. Siegbahn Sweden | 86 | 9.8k 1.0× | 8.3k 1.0× | 5.8k 1.0× | 7.7k 1.4× | 2.2k 0.5× | 464 | 29.9k | ||
| Edward I. Solomon United States | 120 | 30.0k 3.0× | 20.5k 2.4× | 9.5k 1.7× | 13.7k 2.5× | 15.1k 3.4× | 726 | 59.1k | ||
| James E. Penner‐Hahn United States | 66 | 3.7k 0.4× | 4.9k 0.6× | 1.7k 0.3× | 3.5k 0.6× | 2.1k 0.5× | 224 | 13.6k | ||
| Eckhard Bill Germany | 87 | 14.0k 1.4× | 9.5k 1.1× | 6.5k 1.2× | 3.3k 0.6× | 7.0k 1.6× | 557 | 28.4k | ||
| Brian M. Hoffman United States | 85 | 9.9k 1.0× | 11.8k 1.4× | 11.4k 2.0× | 9.2k 1.7× | 2.5k 0.6× | 694 | 33.1k | ||
| Karl Wieghardt Germany | 90 | 16.8k 1.7× | 9.4k 1.1× | 4.0k 0.7× | 2.2k 0.4× | 11.5k 2.5× | 610 | 29.8k | ||
| Harry B. Gray United States | 112 | 12.4k 1.2× | 18.7k 2.2× | 14.1k 2.5× | 11.8k 2.2× | 7.5k 1.7× | 850 | 53.1k | ||
| Stephen P. Cramer United States | 61 | 3.0k 0.3× | 3.2k 0.4× | 4.3k 0.8× | 2.0k 0.4× | 1.1k 0.2× | 270 | 11.0k |
Countries citing papers authored by Keith O. Hodgson
Since
Specialization
Citations
This map shows the geographic impact of Keith O. Hodgson'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 Keith O. Hodgson with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Keith O. Hodgson more than expected).
Fields of papers citing papers by Keith O. Hodgson
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Keith O. Hodgson. 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 Keith O. Hodgson. The network helps show where Keith O. Hodgson may publish in the future.
Co-authorship network of co-authors of Keith O. Hodgson
This figure shows the co-authorship network connecting the top 25 collaborators of Keith O. Hodgson. A scholar is included among the top collaborators of Keith O. Hodgson 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 Keith O. Hodgson. Keith O. Hodgson is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Lim, Hyeongtaek, Mahesh Sundararajan, Yong‐Min Lee, et al.. (2025). Synthesis, Structure, and Redox Reactivity of Ni Complexes Bearing a Redox and Acid–Base Non-innocent Ligand with NiII, NiIII, and NiIV Formal Oxidation States. Journal of the American Chemical Society. 147(5). 3981–3993.
2.
Braun, Augustin, Leland B. Gee, Michael L. Baker, et al.. (2024). Experimental Definition of the S = 1 π vs S = 2 σ Reactivity and S = 2 Character in the Ground State of an S = 1 FeIVO Complex. Journal of the American Chemical Society. 146(51). 35139–35145.
3.
Tao, Lizhi, Hyeongtaek Lim, Yang Ha, et al.. (2023). Tuning the Type 1 Reduction Potential of Multicopper Oxidases: Uncoupling the Effects of Electrostatics and H-Bonding to Histidine Ligands. Journal of the American Chemical Society. 145(24). 13284–13301.
4.
Lee, Chi Chung, Andrew J. Jasniewski, Paul H. Oyala, et al.. (2023). Heterologous synthesis of the complex homometallic cores of nitrogenase P- and M-clusters in Escherichia coli. Proceedings of the National Academy of Sciences. 120(44). e2314788120–e2314788120.
5.
Heyer, Alexander J., Dieter Plessers, Augustin Braun, et al.. (2022). Methane Activation by a Mononuclear Copper Active Site in the Zeolite Mordenite: Effect of Metal Nuclearity on Reactivity. Journal of the American Chemical Society. 144(42). 19305–19316.
6.
Frank, Patrick, Ritimukta Sarangi, Britt Hedman, & Keith O. Hodgson. (2019). Synchrotron X-radiolysis of l -cysteine at the sulfur K-edge: Sulfurous products, experimental surprises, and dioxygen as an oxidoreductant. The Journal of Chemical Physics. 150(10). 105101–105101.
7.
Appel, Mason J., Katlyn K. Meier, Julien Lafrance‐Vanasse, et al.. (2019). Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O 2 activation. Proceedings of the National Academy of Sciences. 116(12). 5370–5375.
8.
Hong, Seungwoo, James J. Yan, Kyle D. Sutherlin, et al.. (2018). A mononuclear nonheme {FeNO}6complex: synthesis and structural and spectroscopic characterization. Chemical Science. 9(34). 6952–6960.
9.
Mara, Michael W., Ryan G. Hadt, Marco Reinhard, et al.. (2017). Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy. Science. 356(6344). 1276–1280.
10.
Frank, Patrick, Róbert K. Szilágyi, Völker Gramlich, et al.. (2017). Spin-Polarization-Induced Preedge Transitions in the Sulfur K-Edge XAS Spectra of Open-Shell Transition-Metal Sulfates: Spectroscopic Validation of σ-Bond Electron Transfer. Inorganic Chemistry. 56(3). 1080–1093.
11.
Antalek, Matthew, E. Pace, Britt Hedman, et al.. (2016). Solvation structure of the halides from x-ray absorption spectroscopy. The Journal of Chemical Physics. 145(4). 44318–44318.
12.
Yan, James J., et al.. (2016). L-Edge X-ray Absorption Spectroscopic Investigation of {FeNO}6: Delocalization vs Antiferromagnetic Coupling. Journal of the American Chemical Society. 139(3). 1215–1225.
13.
Frank, Patrick, et al.. (2015). A high-resolution XAS study of aqueous Cu(II) in liquid and frozen solutions: Pyramidal, polymorphic, and non-centrosymmetric. The Journal of Chemical Physics. 142(8). 84310–84310.
14.
Fay, Aaron W., Michael A. Blank, Chi Chung Lee, et al.. (2011). Spectroscopic Characterization of the Isolated Iron–Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN. Angewandte Chemie International Edition. 50(34). 7787–7790.
15.
Fay, Aaron W., Michael A. Blank, Chi Chung Lee, et al.. (2011). Spectroscopic Characterization of the Isolated Iron–Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN. Angewandte Chemie. 123(34). 7933–7936.
16.
Tenderholt, Adam L., Britt Hedman, & Keith O. Hodgson. (2007). PySpline: A Modern, Cross-Platform Program for the Processing of Raw Averaged XAS Edge and EXAFS Data. AIP conference proceedings. 882. 105–107.
17.
Tenderholt, Adam L., Róbert K. Szilágyi, R. H. Holm, et al.. (2007). Sulfur K-edge XAS of WVO vs. MoVO bis(dithiolene) complexes: Contributions of relativistic effects to electronic structure and reactivity of tungsten enzymes. Journal of Inorganic Biochemistry. 101(11-12). 1594–1600.
18.
Corbett, Mary C., Matthew J. Latimer, T.L. Poulos, et al.. (2007). Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation. Acta Crystallographica Section D Biological Crystallography. 63(9). 951–960.
19.
Corbett, Mary C., F. Akif Tezcan, Oliver Einsle, et al.. (2004). MoK- andL-edge X-ray absorption spectroscopic study of the ADP·AlF4−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal. Journal of Synchrotron Radiation. 12(1). 28–34.
20.
Hedman, Britt, et al.. (1985). Protein microcrystal diffraction and the effects of radiation damage with ultra-high-flux synchrotron radiation.. Proceedings of the National Academy of Sciences. 82(22). 7604–7607.
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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