Timothy E. Machonkin

4.4k total citations · 1 hit paper
22 papers, 3.8k citations indexed

About

Timothy E. Machonkin is a scholar working on Inorganic Chemistry, Molecular Biology and Plant Science. According to data from OpenAlex, Timothy E. Machonkin has authored 22 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Inorganic Chemistry, 10 papers in Molecular Biology and 5 papers in Plant Science. Recurrent topics in Timothy E. Machonkin's work include Metal-Catalyzed Oxygenation Mechanisms (16 papers), Enzyme-mediated dye degradation (5 papers) and Photosynthetic Processes and Mechanisms (5 papers). Timothy E. Machonkin is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (16 papers), Enzyme-mediated dye degradation (5 papers) and Photosynthetic Processes and Mechanisms (5 papers). Timothy E. Machonkin collaborates with scholars based in United States, Italy and South Korea. Timothy E. Machonkin's co-authors include Edward I. Solomon, Uma M. Sundaram, John L. Markley, William M. Westler, Britt Hedman, Keith O. Hodgson, Patrick L. Holland, Daniel J. Kosman, Amy E. Palmer and Scott Severance and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Timothy E. Machonkin

21 papers receiving 3.7k 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.

Multicopper Oxidases and Oxygenases

1996 3.2k citations Edward I. Solomon, Uma M. Sundaram et al. Chemical Reviews profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Timothy E. Machonkin United States	15	1.4k	921	890	874	722	22	3.8k
Uma M. Sundaram United States	4	1.3k 0.9×	851 0.9×	754 0.8×	1.2k 1.4×	653 0.9×	5	3.8k
James W. Whittaker United States	42	2.8k 2.0×	1.2k 1.3×	2.1k 2.4×	850 1.0×	819 1.1×	91	5.8k
Ninian J. Blackburn United States	47	2.4k 1.7×	1.8k 1.9×	2.1k 2.4×	366 0.4×	1.2k 1.7×	141	5.7k
Shinnichiro Suzuki Japan	32	810 0.6×	514 0.6×	1.7k 1.9×	232 0.3×	579 0.8×	176	3.5k
Marius Réglier France	31	1.2k 0.9×	807 0.9×	533 0.6×	171 0.2×	670 0.9×	140	2.9k
Michele Gullotti Italy	33	1.8k 1.3×	1.6k 1.7×	701 0.8×	180 0.2×	847 1.2×	104	3.2k
Udai P. Singh India	29	1.1k 0.7×	868 0.9×	410 0.5×	249 0.3×	793 1.1×	242	3.2k
Angel J. Di Bilio United States	28	692 0.5×	546 0.6×	1.2k 1.3×	111 0.1×	748 1.0×	45	2.8k
Raffaele P. Bonomo Italy	30	532 0.4×	854 0.9×	788 0.9×	297 0.3×	460 0.6×	117	2.8k
Wen Gu China	40	2.4k 1.7×	891 1.0×	1.0k 1.1×	261 0.3×	2.4k 3.4×	241	5.7k

Countries citing papers authored by Timothy E. Machonkin

Since Specialization

Citations

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

Fields of papers citing papers by Timothy E. Machonkin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Timothy E. Machonkin. 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 Timothy E. Machonkin. The network helps show where Timothy E. Machonkin may publish in the future.

Co-authorship network of co-authors of Timothy E. Machonkin

This figure shows the co-authorship network connecting the top 25 collaborators of Timothy E. Machonkin. A scholar is included among the top collaborators of Timothy E. Machonkin 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 Timothy E. Machonkin. Timothy E. Machonkin 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

Vuković, Ivana, et al.. (2019). The role of halogen substituents and substrate pKa in defining the substrate specificity of 2,6-dichlorohydroquinone 1,2-dioxygenase (PcpA). JBIC Journal of Biological Inorganic Chemistry. 24(4). 575–589.

Schofield, Jeremy A., William W. Brennessel, Eugenijus Urnéžius, et al.. (2015). Metal–Halogen Secondary Bonding in a 2,5‐Dichlorohydroquinonate Cobalt(II) Complex: Insight into Substrate Coordination in the Chlorohydroquinone Dioxygenase PcpA. European Journal of Inorganic Chemistry. 2015(28). 4643–4647. 5 indexed citations

Machonkin, Timothy E., Jeremy A. Schofield, Meghan M. Rodriguez, et al.. (2014). Structural and Spectroscopic Characterization of Iron(II), Cobalt(II), and Nickel(II) ortho-Dihalophenolate Complexes: Insights into Metal–Halogen Secondary Bonding. Inorganic Chemistry. 53(18). 9837–9848. 12 indexed citations

Machonkin, Timothy E., et al.. (2011). Substrate Specificity of Sphingobium chlorophenolicum 2,6-Dichlorohydroquinone 1,2-Dioxygenase. Biochemistry. 50(41). 8899–8913. 26 indexed citations

Machonkin, Timothy E., et al.. (2009). Determination of the active site of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA). JBIC Journal of Biological Inorganic Chemistry. 15(3). 291–301. 19 indexed citations

Xia, Bin, et al.. (2009). Hyperfine-Shifted ¹³C and ¹⁵N NMR Signals from Clostridium pasteurianum Rubredoxin: Extensive Assignments and Quantum Chemical Verification. Journal of the American Chemical Society. 131(42). 15555–15563. 19 indexed citations

Brennessel, William W., et al.. (2008). Solid-state and proton NMR characterization of an iron(II) complex of a tridentate, facially coordinating N,N,O donor ligand. Inorganica Chimica Acta. 362(4). 1387–1390. 12 indexed citations

Machonkin, Timothy E., William M. Westler, & John L. Markley. (2005). Paramagnetic NMR Spectroscopy and Density Functional Calculations in the Analysis of the Geometric and Electronic Structures of Iron−Sulfur Proteins. Inorganic Chemistry. 44(4). 779–797. 57 indexed citations

Park, Il Yeong, Marly K. Eidsness, BuHyun Youn, et al.. (2004). Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: Effects of side‐chain size on reduction potential. Proteins Structure Function and Bioinformatics. 57(3). 618–625. 16 indexed citations

10.

Machonkin, Timothy E., William M. Westler, & John L. Markley. (2004). Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates by NMR Spectroscopy: Application to Oxidized Human [2Fe-2S] Ferredoxin. Journal of the American Chemical Society. 126(17). 5413–5426. 38 indexed citations

11.

Machonkin, Timothy E., et al.. (2003). Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin. Journal of the American Chemical Society. 125(6). 1464–1465. 22 indexed citations

12.

Machonkin, Timothy E., William M. Westler, & John L. Markley. (2002). ¹³C{¹³C} 2D NMR: A Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates. Journal of the American Chemical Society. 124(13). 3204–3205. 70 indexed citations

13.

Machonkin, Timothy E., Pulakesh Mukherjee, Mark J. Henson, T. Daniel P. Stack, & Edward I. Solomon. (2002). The EPR spectrum of a Cu(II/II/III) cluster: anisotropic exchange in a bent Cu(II)2O2 core. Inorganica Chimica Acta. 341. 39–44. 19 indexed citations

14.

Machonkin, Timothy E., Liliana Quintanar, Amy E. Palmer, et al.. (2001). Spectroscopy and Reactivity of the Type 1 Copper Site in Fet3p from Saccharomyces cerevisiae: Correlation of Structure with Reactivity in the Multicopper Oxidases. Journal of the American Chemical Society. 123(23). 5507–5517. 66 indexed citations

15.

Machonkin, Timothy E. & Edward I. Solomon. (2000). The Thermodynamics, Kinetics, and Molecular Mechanism of Intramolecular Electron Transfer in Human Ceruloplasmin. Journal of the American Chemical Society. 122(50). 12547–12560. 67 indexed citations

16.

Machonkin, Timothy E., Giovanni Musci, Maria Carmela Bonaccorsi di Patti, et al.. (1999). Investigation of the Anomalous Spectroscopic Features of the Copper Sites in Chicken Ceruloplasmin: Comparison to Human Ceruloplasmin. Biochemistry. 38(34). 11093–11102. 5 indexed citations

17.

Machonkin, Timothy E., et al.. (1998). Spectroscopic and Magnetic Studies of Human Ceruloplasmin: Identification of a Redox-Inactive Reduced Type 1 Copper Site. Biochemistry. 37(26). 9570–9578. 64 indexed citations

18.

Solomon, Edward I., Uma M. Sundaram, & Timothy E. Machonkin. (1997). ChemInform Abstract: Multicopper Oxidases and Oxygenases. ChemInform. 28(10). 1 indexed citations

19.

Solomon, Edward I., Uma M. Sundaram, & Timothy E. Machonkin. (1996). Multicopper Oxidases and Oxygenases. Chemical Reviews. 96(7). 2563–2606. 3166 indexed citations breakdown →

20.

Law, Neil A., et al.. (1995). A structurally characterized dichloro-manganese(IV) complex capable of halogenating alkenes. Journal of the Chemical Society Chemical Communications. 2015–2015. 22 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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