Basem Soboh

1.1k total citations
24 papers, 822 citations indexed

About

Basem Soboh is a scholar working on Renewable Energy, Sustainability and the Environment, Inorganic Chemistry and Molecular Biology. According to data from OpenAlex, Basem Soboh has authored 24 papers receiving a total of 822 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Renewable Energy, Sustainability and the Environment, 9 papers in Inorganic Chemistry and 6 papers in Molecular Biology. Recurrent topics in Basem Soboh's work include Metalloenzymes and iron-sulfur proteins (24 papers), Electrocatalysts for Energy Conversion (17 papers) and Metal-Catalyzed Oxygenation Mechanisms (9 papers). Basem Soboh is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (24 papers), Electrocatalysts for Energy Conversion (17 papers) and Metal-Catalyzed Oxygenation Mechanisms (9 papers). Basem Soboh collaborates with scholars based in Germany, United States and United Kingdom. Basem Soboh's co-authors include Reiner Hedderich, Dietmar Linder, R. Gary Sawers, Luis M. Rubio, Sven T. Stripp, Robert Y. Igarashi, José A. Hernández, Leonardo Curatti, Dehua Zhao and Ute Lindenstrauß 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

Basem Soboh

24 papers receiving 817 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Basem Soboh Germany 18 601 257 176 164 119 24 822
Pierre-Pol Liebgott France 18 621 1.0× 263 1.0× 127 0.7× 149 0.9× 64 0.5× 33 1.0k
Constanze Pinske Germany 16 475 0.8× 380 1.5× 183 1.0× 148 0.9× 92 0.8× 36 778
И. Н. Гоготов Russia 16 377 0.6× 251 1.0× 152 0.9× 72 0.4× 26 0.2× 43 647
Simone Morra Italy 13 333 0.6× 92 0.4× 82 0.5× 83 0.5× 49 0.4× 21 487
К. Болатхан Kazakhstan 13 379 0.6× 148 0.6× 121 0.7× 98 0.6× 12 0.1× 29 632
Nicole Forget France 12 373 0.6× 191 0.7× 76 0.4× 124 0.8× 53 0.4× 15 546
Ki-Seok Yoon Japan 14 265 0.4× 195 0.8× 62 0.4× 81 0.5× 88 0.7× 35 503
Lucia Forzi Germany 5 234 0.4× 202 0.8× 102 0.6× 86 0.5× 27 0.2× 6 419
Alexander F. Arendsen Netherlands 12 286 0.5× 160 0.6× 41 0.2× 104 0.6× 117 1.0× 19 470
L L Lundie United States 9 151 0.3× 328 1.3× 62 0.4× 117 0.7× 73 0.6× 9 617

Countries citing papers authored by Basem Soboh

Since Specialization
Citations

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

Fields of papers citing papers by Basem Soboh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Basem Soboh. 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 Basem Soboh. The network helps show where Basem Soboh may publish in the future.

Co-authorship network of co-authors of Basem Soboh

This figure shows the co-authorship network connecting the top 25 collaborators of Basem Soboh. A scholar is included among the top collaborators of Basem Soboh 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 Basem Soboh. Basem Soboh 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.
Soboh, Basem, Lorenz Adrian, & Sven T. Stripp. (2022). An in vitro reconstitution system to monitor iron transfer to the active site during the maturation of [NiFe]-hydrogenase. Journal of Biological Chemistry. 298(9). 102291–102291. 4 indexed citations
2.
Stripp, Sven T., Christina S. Müller, D. Ehrenberg, et al.. (2021). Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly. Biochemical Journal. 478(17). 3281–3295. 6 indexed citations
3.
Senger, Moritz, Konstantin Laun, Basem Soboh, & Sven T. Stripp. (2018). Infrared Characterization of the Bidirectional Oxygen-Sensitive [NiFe]-Hydrogenase from E. coli. Catalysts. 8(11). 530–530. 5 indexed citations
4.
Senger, Moritz, Sven T. Stripp, & Basem Soboh. (2017). Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis. Journal of Biological Chemistry. 292(28). 11670–11681. 23 indexed citations
5.
Stripp, Sven T., Ute Lindenstrauß, R. Gary Sawers, & Basem Soboh. (2015). Identification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl–Group Channeling during [NiFe]–Hydrogenase Cofactor Generation. PLoS ONE. 10(7). e0133118–e0133118. 10 indexed citations
6.
Stripp, Sven T., et al.. (2014). The Influence of Oxygen on [NiFe]–Hydrogenase Cofactor Biosynthesis and How Ligation of Carbon Monoxide Precedes Cyanation. PLoS ONE. 9(9). e107488–e107488. 17 indexed citations
7.
Soboh, Basem, Sven T. Stripp, Ute Lindenstrauß, et al.. (2013). The [NiFe]‐hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron‐ and carbon dioxide‐binding proteins. FEBS Letters. 587(16). 2512–2516. 34 indexed citations
8.
Stripp, Sven T., Basem Soboh, Ute Lindenstrauß, et al.. (2013). HypD Is the Scaffold Protein for Fe-(CN)2CO Cofactor Assembly in [NiFe]-Hydrogenase Maturation. Biochemistry. 52(19). 3289–3296. 44 indexed citations
9.
Soboh, Basem, et al.. (2012). [NiFe]‐hydrogenase maturation: Isolation of a HypC–HypD complex carrying diatomic CO and CN− ligands. FEBS Letters. 586(21). 3882–3887. 34 indexed citations
10.
Trchounian, Karen, Basem Soboh, R. Gary Sawers, & Armen Trchоunian. (2012). Contribution of Hydrogenase 2 to Stationary Phase H2 Production by Escherichia coli During Fermentation of Glycerol. Cell Biochemistry and Biophysics. 66(1). 103–108. 25 indexed citations
11.
Soboh, Basem, et al.. (2012). Evidence for an oxygen-sensitive iron–sulfur cluster in an immature large subunit species of Escherichia coli [NiFe]-hydrogenase 2. Biochemical and Biophysical Research Communications. 424(1). 158–163. 12 indexed citations
12.
Shi, Rong, Yunge Li, Christine Munger, et al.. (2011). Structure of Hydrogenase Maturation Protein HypF with Reaction Intermediates Shows Two Active Sites. Structure. 19(12). 1773–1783. 30 indexed citations
13.
Soboh, Basem, Constanze Pinske, Martin Kuhns, et al.. (2011). The respiratory molybdo-selenoprotein formate dehydrogenases of Escherichia coli have hydrogen: benzyl viologen oxidoreductase activity. BMC Microbiology. 11(1). 173–173. 48 indexed citations
14.
Pinske, Constanze, Basem Soboh, Christian Ihling, et al.. (2011). Efficient electron transfer from hydrogen to benzyl viologen by the [NiFe]-hydrogenases of Escherichia coli is dependent on the coexpression of the iron–sulfur cluster-containing small subunit. Archives of Microbiology. 193(12). 893–903. 47 indexed citations
15.
Soboh, Basem, Eric S. Boyd, Dehua Zhao, John W. Peters, & Luis M. Rubio. (2010). Substrate specificity and evolutionary implications of a NifDK enzyme carrying NifB‐co at its active site. FEBS Letters. 584(8). 1487–1492. 29 indexed citations
16.
Soboh, Basem, et al.. (2010). Development of a cell‐free system reveals an oxygen‐labile step in the maturation of [NiFe]‐hydrogenase 2 of Escherichia coli. FEBS Letters. 584(18). 4109–4114. 18 indexed citations
17.
George, Simon J., Robert Y. Igarashi, Cínthia Piamonteze, et al.. (2007). Identification of a Mo−Fe−S Cluster on NifEN by Mo K-Edge Extended X-ray Absorption Fine Structure. Journal of the American Chemical Society. 129(11). 3060–3061. 15 indexed citations
18.
Soboh, Basem, Robert Y. Igarashi, José A. Hernández, & Luis M. Rubio. (2006). Purification of a NifEN Protein Complex That Contains Bound Molybdenum and a FeMo-Co Precursor from an Azotobacter vinelandii ΔnifHDK Strain. Journal of Biological Chemistry. 281(48). 36701–36709. 22 indexed citations
19.
Hernández, José A., Robert Y. Igarashi, Basem Soboh, et al.. (2006). NifX and NifEN exchange NifB cofactor and the VK‐cluster, a newly isolated intermediate of the iron‐molybdenum cofactor biosynthetic pathway. Molecular Microbiology. 63(1). 177–192. 56 indexed citations
20.
Soboh, Basem, Dietmar Linder, & Reiner Hedderich. (2002). Purification and catalytic properties of a CO‐oxidizing:H2‐evolving enzyme complex from Carboxydothermus hydrogenoformans. European Journal of Biochemistry. 269(22). 5712–5721. 88 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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