John D. Lipscomb

19.2k total citations · 2 hit papers
222 papers, 14.9k citations indexed

About

John D. Lipscomb is a scholar working on Inorganic Chemistry, Molecular Biology and Pollution. According to data from OpenAlex, John D. Lipscomb has authored 222 papers receiving a total of 14.9k indexed citations (citations by other indexed papers that have themselves been cited), including 169 papers in Inorganic Chemistry, 151 papers in Molecular Biology and 44 papers in Pollution. Recurrent topics in John D. Lipscomb's work include Metal-Catalyzed Oxygenation Mechanisms (169 papers), Microbial metabolism and enzyme function (66 papers) and Microbial bioremediation and biosurfactants (44 papers). John D. Lipscomb is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (169 papers), Microbial metabolism and enzyme function (66 papers) and Microbial bioremediation and biosurfactants (44 papers). John D. Lipscomb collaborates with scholars based in United States, Russia and Japan. John D. Lipscomb's co-authors include Bradley J. Wallar, Elena G. Kovaleva, Eckard Münck, Lawrence Que, Allen M. Orville, Jeremy C. Nesheim, D.H. Ohlendorf, Brian G. Fox, Wayne A. Froland and I. C. Gunsalus and has published in prestigious journals such as Nature, Science and Chemical Reviews.

In The Last Decade

John D. Lipscomb

222 papers receiving 14.6k 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.

Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters

1996 1.1k citations Bradley J. Wallar, John D. Lipscomb profile →
Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

2008 541 citations Elena G. Kovaleva, John D. Lipscomb profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
John D. Lipscomb United States	69	10.6k	7.4k	3.6k	2.6k	2.5k	222	14.9k
J. Martin Bollinger United States	63	8.9k 0.8×	6.3k 0.8×	2.8k 0.8×	643 0.3×	2.6k 1.1×	197	12.7k
Carsten Krebs United States	68	8.8k 0.8×	7.0k 0.9×	3.1k 0.8×	609 0.2×	2.4k 1.0×	205	14.2k
Sam P. de Visser United Kingdom	76	12.7k 1.2×	5.9k 0.8×	5.8k 1.6×	491 0.2×	3.4k 1.3×	327	18.2k
Eckard Münck United States	82	12.8k 1.2×	6.4k 0.9×	6.5k 1.8×	719 0.3×	4.5k 1.8×	278	20.9k
Amy C. Rosenzweig United States	63	4.5k 0.4×	5.9k 0.8×	2.6k 0.7×	1.1k 0.4×	2.6k 1.0×	160	12.5k
José J. G. Moura Portugal	65	4.2k 0.4×	5.9k 0.8×	3.2k 0.9×	876 0.3×	1.2k 0.5×	491	16.0k
Hans Eklund Sweden	52	3.4k 0.3×	6.5k 0.9×	2.4k 0.6×	662 0.3×	1.4k 0.6×	109	10.0k
Judith P. Klinman United States	71	4.6k 0.4×	10.0k 1.3×	2.7k 0.7×	187 0.1×	1.3k 0.5×	281	16.7k
Yoshihito Watanabe Japan	60	5.2k 0.5×	4.0k 0.5×	3.0k 0.8×	142 0.1×	1.7k 0.7×	267	10.8k
Devesh Kumar India	49	6.0k 0.6×	2.4k 0.3×	2.9k 0.8×	188 0.1×	1.6k 0.7×	169	8.6k

Countries citing papers authored by John D. Lipscomb

Since Specialization

Citations

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

Fields of papers citing papers by John D. Lipscomb

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John D. Lipscomb. 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 John D. Lipscomb. The network helps show where John D. Lipscomb may publish in the future.

Co-authorship network of co-authors of John D. Lipscomb

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Cutsail, George E., et al.. (2022). Determination of the iron(IV) local spin states of the Q intermediate of soluble methane monooxygenase by Kβ X-ray emission spectroscopy. JBIC Journal of Biological Inorganic Chemistry. 27(6). 573–582. 7 indexed citations

Shah, Rachit, Melanie S. Rogers, David Wang, et al.. (2022). Dynamic Long-Range Interactions Influence Substrate Binding and Catalysis by Human Histidine Triad Nucleotide-Binding Proteins (HINTs), Key Regulators of Multiple Cellular Processes and Activators of Antiviral ProTides. Biochemistry. 61(23). 2648–2661. 1 indexed citations

Sutherlin, Kyle D., Yuko Wasada‐Tsutsui, Michael M. Mbughuni, et al.. (2018). Nuclear Resonance Vibrational Spectroscopy Definition of O₂ Intermediates in an Extradiol Dioxygenase: Correlation to Crystallography and Reactivity. Journal of the American Chemical Society. 140(48). 16495–16513. 19 indexed citations

Finzel, B.C., et al.. (2017). Rational Optimization of Mechanism-Based Inhibitors through Determination of the Microscopic Rate Constants of Inactivation. Journal of the American Chemical Society. 139(21). 7132–7135. 11 indexed citations

Banerjee, R., Anna J. Komor, & John D. Lipscomb. (2017). Use of Isotopes and Isotope Effects for Investigations of Diiron Oxygenase Mechanisms. Methods in enzymology on CD-ROM/Methods in enzymology. 596. 239–290. 11 indexed citations

Komor, Anna J., et al.. (2017). CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates. Biochemistry. 56(37). 4940–4950. 22 indexed citations

Fielding, Andrew J., John D. Lipscomb, & Lawrence Que. (2014). A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases. JBIC Journal of Biological Inorganic Chemistry. 19(4-5). 491–504. 38 indexed citations

Mbughuni, Michael M., Mrinmoy Chakrabarti, Joshua A. Hayden, et al.. (2010). Trapping and spectroscopic characterization of an Fe^III-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proceedings of the National Academy of Sciences. 107(39). 16788–16793. 134 indexed citations

Lipscomb, John D.. (2009). PL. Plenary lectures. JBIC Journal of Biological Inorganic Chemistry. 14(S1). 5–7. 1 indexed citations

10.

Kovaleva, Elena G. & John D. Lipscomb. (2007). Crystal Structures of Fe ²⁺ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates. Science. 316(5823). 453–457. 321 indexed citations

11.

Jin, Yi & John D. Lipscomb. (2000). Mechanistic insights into C–H activation from radical clock chemistry: oxidation of substituted methylcyclopropanes catalyzed by soluble methane monooxygenase from Methylosinus trichosporium OB3b. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1543(1). 47–59. 21 indexed citations

12.

Wallar, Bradley J., et al.. (1999). Solution Structure of Component B from Methane Monooxygenase Derived through Heteronuclear NMR and Molecular Modeling^,. Biochemistry. 38(18). 5799–5812. 45 indexed citations

13.

Davis, Mindy I., Erik C. Wasinger, Tami E. Westre, et al.. (1999). Spectroscopic Investigation of Reduced Protocatechuate 3,4-Dioxygenase: Charge-Induced Alterations in the Active Site Iron Coordination Environment. Inorganic Chemistry. 38(16). 3676–3683. 13 indexed citations

14.

Radhakrishnan, R., et al.. (1997). Crystal structure of the hydroxylase component of methane monooxygenase fromMethylosinus trichosporiumOB3b. Protein Science. 6(3). 556–568. 226 indexed citations

15.

Liu, Yi, Jeremy C. Nesheim, Kim Paulsen, Marian T. Stankovich, & John D. Lipscomb. (1997). Roles of the Methane Monooxygenase Reductase Component in the Regulation of Catalysis. Biochemistry. 36(17). 5223–5233. 35 indexed citations

16.

Orville, Allen M. & John D. Lipscomb. (1993). Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase.. Journal of Biological Chemistry. 268(12). 8596–8607. 47 indexed citations

17.

Andersson, K. Kristoffer, Wayne A. Froland, Sang‐Kyu Lee, & John D. Lipscomb. (1991). Dioxygen independent oxygenation of hydrocarbons by methane monooxygenae hydroxylase component. New Journal of Chemistry. 15(6). 411–415. 65 indexed citations

18.

Lipscomb, John D., et al.. (1990). [16] Protocatechuate 2,3-dioxygenase from Bacillus macerans. Methods in enzymology on CD-ROM/Methods in enzymology. 188. 95–101. 13 indexed citations

19.

Arciero, D.M. & John D. Lipscomb. (1986). Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases.. Journal of Biological Chemistry. 261(5). 2170–2178. 125 indexed citations

20.

Lipscomb, John D. & I. C. Gunsalus. (1973). STRUCTURAL ASPECTS OF THE ACTIVE SITE OF CYTOCHROME P-45Ocam. Drug Metabolism and Disposition. 1(1). 1–5. 3 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.

Explore authors with similar magnitude of impact