Robert C. Scarrow

1.6k total citations
31 papers, 1.4k citations indexed

About

Robert C. Scarrow is a scholar working on Inorganic Chemistry, Molecular Biology and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, Robert C. Scarrow has authored 31 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Inorganic Chemistry, 9 papers in Molecular Biology and 9 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in Robert C. Scarrow's work include Metal-Catalyzed Oxygenation Mechanisms (8 papers), Metalloenzymes and iron-sulfur proteins (7 papers) and Metal complexes synthesis and properties (6 papers). Robert C. Scarrow is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (8 papers), Metalloenzymes and iron-sulfur proteins (7 papers) and Metal complexes synthesis and properties (6 papers). Robert C. Scarrow collaborates with scholars based in United States, Denmark and Australia. Robert C. Scarrow's co-authors include Kenneth N. Raymond, David L. White, Mark Nelson, Lawrence Que, Julie A. Kovacs, Bridget A. Brennan, Jason Shearer, Kamal Abu-Dari, Paul E. Riley and A. S. Borovik 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

Robert C. Scarrow

31 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert C. Scarrow United States 21 634 437 429 341 282 31 1.4k
Scot Wherland United States 26 517 0.8× 241 0.6× 695 1.6× 512 1.5× 354 1.3× 77 2.0k
Antonio Donaire Spain 24 334 0.5× 453 1.0× 772 1.8× 398 1.2× 349 1.2× 62 1.6k
James L. Corbin United States 24 364 0.6× 312 0.7× 265 0.6× 228 0.7× 469 1.7× 45 1.4k
A. Graham Lappin United States 22 543 0.9× 542 1.2× 230 0.5× 715 2.1× 374 1.3× 104 1.6k
Deyuan Kong United States 22 524 0.8× 334 0.8× 186 0.4× 374 1.1× 323 1.1× 70 1.4k
Takehiko Tosha Japan 32 1.1k 1.7× 444 1.0× 1.0k 2.4× 758 2.2× 332 1.2× 87 2.7k
Jake W. Ginsbach United States 12 1.3k 2.0× 721 1.6× 425 1.0× 701 2.1× 498 1.8× 14 2.1k
Christian H. Kjaergaard United States 13 1.0k 1.7× 547 1.3× 544 1.3× 645 1.9× 379 1.3× 14 2.3k
Gerard J. Colpas United States 17 1.0k 1.6× 408 0.9× 291 0.7× 521 1.5× 437 1.5× 19 1.7k
Esther M. Johnston United States 9 975 1.5× 514 1.2× 582 1.4× 520 1.5× 363 1.3× 9 2.0k

Countries citing papers authored by Robert C. Scarrow

Since Specialization
Citations

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

Fields of papers citing papers by Robert C. Scarrow

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert C. Scarrow. 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 Robert C. Scarrow. The network helps show where Robert C. Scarrow may publish in the future.

Co-authorship network of co-authors of Robert C. Scarrow

This figure shows the co-authorship network connecting the top 25 collaborators of Robert C. Scarrow. A scholar is included among the top collaborators of Robert C. Scarrow 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 Robert C. Scarrow. Robert C. Scarrow 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.
Yap, Glenn P. A., et al.. (2010). Trigonal Bi- and Monopyramidal Cobalt(II) Complexes of a Novel Guanidine-Based Tripodal Ligand. Inorganic Chemistry. 49(24). 11261–11263. 12 indexed citations
2.
Scarrow, Robert C., et al.. (2004). Development of porous materials for heterogeneous catalysis: kinetic resolution of epoxides. Chemical Communications. 2544–2544. 21 indexed citations
3.
Shearer, Jason, et al.. (2003). How does cyanide inhibit superoxide reductase? Insight from synthetic Fe III N 4 S model complexes. Proceedings of the National Academy of Sciences. 100(7). 3671–3676. 39 indexed citations
4.
Shearer, Jason, Robert C. Scarrow, & Julie A. Kovacs. (2002). Synthetic Models for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase:  Observation and Structural Characterization by XAS of an FeIII−OOH Intermediate. Journal of the American Chemical Society. 124(39). 11709–11717. 78 indexed citations
5.
Shearer, Jason, Henry L. Jackson, Dirk Schweitzer, et al.. (2002). The First Example of a Nitrile Hydratase Model Complex that Reversibly Binds Nitriles. Journal of the American Chemical Society. 124(38). 11417–11428. 42 indexed citations
6.
Hazell, A., et al.. (2002). A Dihydroxo-Bridged Fe(II)−Fe(III) Complex:  A New Member of the Diiron Diamond Core Family. Journal of the American Chemical Society. 125(1). 32–33. 24 indexed citations
7.
MacBeth, C.E., et al.. (2001). Immobilized Metal Complexes in Porous Organic Hosts:  Development of a Material for the Selective and Reversible Binding of Nitric Oxide. Journal of the American Chemical Society. 123(6). 1072–1079. 67 indexed citations
8.
Kervinen, Jukka, Roland L. Dunbrack, Samuel Litwin, et al.. (2000). Porphobilinogen Synthase from Pea:  Expression from an Artificial Gene, Kinetic Characterization, and Novel Implications for Subunit Interactions. Biochemistry. 39(30). 9018–9029. 37 indexed citations
9.
Zentko, Suzanne, Robert C. Scarrow, Wayne W. Wright, & Jane M. Vanderkooi. (1999). Protonation of porphyrin in iron-free cytochromec: Spectral properties of monocation free base porphyrin, a charge analogue of ferric heme. Biospectroscopy. 5(3). 141–150. 7 indexed citations
10.
Ryle, Matthew J., William N. Lanzilotta, Lance C. Seefeldt, Robert C. Scarrow, & Gerard M. Jensen. (1996). Circular Dichroism and X-ray Spectroscopies of Azotobacter vinelandii Nitrogenase Iron Protein. Journal of Biological Chemistry. 271(3). 1551–1557. 41 indexed citations
11.
Brennan, Bridget A., et al.. (1996). Nitrile Hydratase from Rhodococcus rhodochrous J1 Contains a Non-Corrin Cobalt Ion with Two Sulfur Ligands. Journal of the American Chemical Society. 118(38). 9194–9195. 108 indexed citations
12.
Nelson, Mark, et al.. (1995). Structure and Kinetics of Formation of Catechol Complexes of Ferric Soybean Lipoxygenase-1. Biochemistry. 34(46). 15219–15229. 14 indexed citations
13.
Scarrow, Robert C., et al.. (1994). X-ray Spectroscopy of the Iron Site in Soybean Lipoxygenase-1: Changes in Coordination upon Oxidation or Addition of Methanol. Biochemistry. 33(50). 15023–15035. 92 indexed citations
14.
True, Anne E., Robert C. Scarrow, Clayton R. Randall, Richard C. Holz, & Lawrence Que. (1993). EXAFS studies of uteroferrin and its anion complexes. Journal of the American Chemical Society. 115(10). 4246–4255. 66 indexed citations
15.
Brennan, Bridget A., Haiyong Jin, D. Bruce Chase, et al.. (1993). Nitrile hydratase: A novel iron-sulfur center. Journal of Inorganic Biochemistry. 51(1-2). 374–374. 4 indexed citations
16.
Scarrow, Robert C. & Kenneth N. Raymond. (1988). Ferric ion sequestering agents. 19. Synthesis of N-alkyl-3-hydroxy-2(1H)-pyridinones and coordination complexes with iron(III). Inorganic Chemistry. 27(23). 4140–4149. 26 indexed citations
17.
Turowski, Petra N., Steven J. Rodgers, Robert C. Scarrow, & Kenneth N. Raymond. (1988). Ferric ion sequestering agents. 18. Two dihydroxamic acid derivatives of EDTA and DTPA. Inorganic Chemistry. 27(3). 474–481. 37 indexed citations
18.
Scarrow, Robert C., Michael J. Maroney, Sharon M. Palmer, et al.. (1986). EXAFS studies of the B2 subunit of the ribonucleotide reductase from E. coli. Journal of the American Chemical Society. 108(21). 6832–6834. 19 indexed citations
19.
Scarrow, Robert C., Paul E. Riley, Kamal Abu-Dari, David L. White, & Kenneth N. Raymond. (1985). Ferric ion sequestering agents. 13. Synthesis, structures, and thermodynamics of complexation of cobalt(III) and iron(III) tris complexes of several chelating hydroxypyridinones. Inorganic Chemistry. 24(6). 954–967. 136 indexed citations
20.
Borgias, Brandan A., et al.. (1985). sym-Triphenylcyclopropenylium hexabromotellurate(IV), (C21H15)2[TeBr6]. Acta Crystallographica Section C Crystal Structure Communications. 41(3). 476–479. 2 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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