Richard A. Rothery

3.8k total citations
70 papers, 3.2k citations indexed

About

Richard A. Rothery is a scholar working on Renewable Energy, Sustainability and the Environment, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Richard A. Rothery has authored 70 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Renewable Energy, Sustainability and the Environment, 39 papers in Molecular Biology and 32 papers in Inorganic Chemistry. Recurrent topics in Richard A. Rothery's work include Metalloenzymes and iron-sulfur proteins (45 papers), Metal-Catalyzed Oxygenation Mechanisms (32 papers) and Photosynthetic Processes and Mechanisms (27 papers). Richard A. Rothery is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (45 papers), Metal-Catalyzed Oxygenation Mechanisms (32 papers) and Photosynthetic Processes and Mechanisms (27 papers). Richard A. Rothery collaborates with scholars based in Canada, United States and France. Richard A. Rothery's co-authors include Joël H. Weiner, Francis Blasco, N.C.J. Strynadka, Michela G. Bertero, Richard Schulz, Péter Ferdinandy, Catharine A. Trieber, Axel Magalon, Elena Maklashina and Gary Cecchini and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Richard A. Rothery

69 papers receiving 3.2k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Richard A. Rothery Canada 34 1.5k 1.5k 787 410 297 70 3.2k
R. N. F. Thorneley United Kingdom 41 2.1k 1.4× 1.8k 1.3× 833 1.1× 944 2.3× 321 1.1× 122 5.7k
Maria João Romão Portugal 43 2.7k 1.8× 2.1k 1.4× 1.4k 1.8× 858 2.1× 255 0.9× 182 6.1k
Javier Seravalli United States 36 1.9k 1.2× 987 0.7× 615 0.8× 343 0.8× 87 0.3× 76 3.8k
Dennis H. Flint United States 20 1.4k 0.9× 1.1k 0.7× 419 0.5× 397 1.0× 160 0.5× 31 2.6k
Jean‐Marc Moulis France 31 1.1k 0.7× 990 0.7× 655 0.8× 402 1.0× 78 0.3× 94 3.1k
William H. Orme‐Johnson United States 50 2.5k 1.6× 2.5k 1.7× 1.3k 1.6× 964 2.4× 294 1.0× 136 6.3k
Carlos D. Brondino Argentina 31 535 0.4× 898 0.6× 754 1.0× 576 1.4× 209 0.7× 91 2.5k
Ulrich Ermler Germany 31 2.3k 1.5× 641 0.4× 602 0.8× 662 1.6× 160 0.5× 74 3.6k
Stephen G. Mayhew Ireland 37 3.3k 2.2× 732 0.5× 577 0.7× 1.1k 2.7× 160 0.5× 116 5.3k
Sean J. Elliott United States 31 1.5k 1.0× 986 0.7× 729 0.9× 444 1.1× 494 1.7× 90 3.2k

Countries citing papers authored by Richard A. Rothery

Since Specialization
Citations

This map shows the geographic impact of Richard A. Rothery'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 Richard A. Rothery with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Richard A. Rothery more than expected).

Fields of papers citing papers by Richard A. Rothery

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard A. Rothery. 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 Richard A. Rothery. The network helps show where Richard A. Rothery may publish in the future.

Co-authorship network of co-authors of Richard A. Rothery

This figure shows the co-authorship network connecting the top 25 collaborators of Richard A. Rothery. A scholar is included among the top collaborators of Richard A. Rothery 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 Richard A. Rothery. Richard A. Rothery is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Rothery, Richard A. & Joël H. Weiner. (2014). Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination. JBIC Journal of Biological Inorganic Chemistry. 20(2). 349–372. 36 indexed citations
2.
Rothery, Richard A., et al.. (2013). A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827(6). 730–737. 9 indexed citations
3.
Rothery, Richard A., Benjamin W. Stein, Matthew Solomonson, Martin L. Kirk, & Joël H. Weiner. (2012). Pyranopterin conformation defines the function of molybdenum and tungsten enzymes. Proceedings of the National Academy of Sciences. 109(37). 14773–14778. 81 indexed citations
4.
Ruprecht, Jonathan J., So Iwata, Richard A. Rothery, et al.. (2011). Perturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur Cluster. Journal of Biological Chemistry. 286(14). 12756–12765. 27 indexed citations
5.
Pushie, M. Jake, et al.. (2010). Molybdenum Site Structure of Escherichia coli YedY, a Novel Bacterial Oxidoreductase. Inorganic Chemistry. 50(3). 732–740. 18 indexed citations
6.
Maklashina, Elena, T.M. Iverson, Juni Andréll, et al.. (2006). Fumarate Reductase and Succinate Oxidase Activity of Escherichia coli Complex II Homologs Are Perturbed Differently by Mutation of the Flavin Binding Domain. Journal of Biological Chemistry. 281(16). 11357–11365. 49 indexed citations
7.
Zhao, Zhongwei, et al.. (2006). The Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow. Journal of Biological Chemistry. 281(37). 27662–27668. 46 indexed citations
8.
Rothery, Richard A., Andrew Spiers, Elena Maklashina, et al.. (2004). Defining the QP‐site of Escherichia coli fumarate reductase by site‐directed mutagenesis, fluorescence quench titrations and EPR spectroscopy. FEBS Journal. 272(2). 313–326. 22 indexed citations
9.
Bertero, Michela G., Richard A. Rothery, Francis Blasco, et al.. (2004). Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A. Journal of Biological Chemistry. 280(15). 14836–14843. 65 indexed citations
10.
Bertero, Michela G., Richard A. Rothery, Huiying Hou, et al.. (2003). Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nature Structural & Molecular Biology. 10(9). 681–687. 399 indexed citations
11.
12.
Elliott, Sean J., Christophe Léger, Judy Hirst, et al.. (2002). Detection and interpretation of redox potential optima in the catalytic activity of enzymes. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1555(1-3). 54–59. 41 indexed citations
13.
Damaraju, Sambasivarao, et al.. (2002). Differential effects of a molybdopterin synthase sulfurylase (moeB) mutation on Escherichia coli molybdoenzyme maturation. Biochemistry and Cell Biology. 80(4). 435–443. 13 indexed citations
14.
Maklashina, Elena, Richard A. Rothery, Joël H. Weiner, & Gary Cecchini. (2001). Retention of Heme in Axial Ligand Mutants of Succinate-Ubiquinone Oxidoreductase (Complex II) from Escherichia coli. Journal of Biological Chemistry. 276(22). 18968–18976. 40 indexed citations
15.
16.
Rothery, Richard A. & Joël H. Weiner. (1998). Interaction of a menaquinol binding site with the [3Fe‐4S] cluster of Escherichia coli fumarate reductase. European Journal of Biochemistry. 254(3). 588–595. 25 indexed citations
17.
Rothery, Richard A., Axel Magalon, Gérard Giordano, et al.. (1998). The Molybdenum Cofactor of Escherichia coli Nitrate Reductase A (NarGHI). Journal of Biological Chemistry. 273(13). 7462–7469. 50 indexed citations
18.
Rothery, Richard A., et al.. (1994). The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria. European Journal of Biochemistry. 222(3). 983–990. 44 indexed citations
19.
Turner, Raymond J., Diane E. Taylor, Richard A. Rothery, & Joël H. Weiner. (1993). Easy method for SDS-PAGE gel drying and preservation.. PubMed. 14(2). 200–1. 1 indexed citations
20.
Weiner, Joël H., Richard A. Rothery, Sambasivarao Damaraju, & Catharine A. Trieber. (1992). Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1102(1). 1–18. 113 indexed citations

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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