Luis M. Rubio

4.2k total citations
72 papers, 2.7k citations indexed

About

Luis M. Rubio is a scholar working on Renewable Energy, Sustainability and the Environment, Molecular Biology and Catalysis. According to data from OpenAlex, Luis M. Rubio has authored 72 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 62 papers in Renewable Energy, Sustainability and the Environment, 22 papers in Molecular Biology and 19 papers in Catalysis. Recurrent topics in Luis M. Rubio's work include Metalloenzymes and iron-sulfur proteins (60 papers), Electrocatalysts for Energy Conversion (28 papers) and Ammonia Synthesis and Nitrogen Reduction (19 papers). Luis M. Rubio is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (60 papers), Electrocatalysts for Energy Conversion (28 papers) and Ammonia Synthesis and Nitrogen Reduction (19 papers). Luis M. Rubio collaborates with scholars based in Spain, United States and United Kingdom. Luis M. Rubio's co-authors include Paul W. Ludden, Leonardo Curatti, Stefan Burén, Enrique Flores, Antonia Herrero, Carlos Echávarri‐Erasun, José A. Hernández, Emilio Jiménez‐Vicente, José E. Frías and Gema López‐Torrejón 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

Luis M. Rubio

70 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Luis M. Rubio Spain 29 1.7k 781 655 620 395 72 2.7k
Paul E. Bishop United States 24 1.3k 0.8× 618 0.8× 436 0.7× 421 0.7× 476 1.2× 44 2.2k
G P Roberts United States 30 1.1k 0.7× 1.3k 1.6× 365 0.6× 229 0.4× 472 1.2× 50 2.6k
H. Haaker Netherlands 25 940 0.6× 617 0.8× 319 0.5× 271 0.4× 227 0.6× 57 1.7k
Robert H. Burris United States 21 721 0.4× 525 0.7× 1.1k 1.6× 299 0.5× 180 0.5× 41 2.3k
Bernard Billoud France 14 1.5k 0.9× 846 1.1× 216 0.3× 113 0.2× 421 1.1× 29 2.6k
Yves Jouanneau France 31 667 0.4× 1.1k 1.5× 228 0.3× 111 0.2× 411 1.0× 66 2.4k
R L Robson United Kingdom 18 638 0.4× 457 0.6× 288 0.4× 131 0.2× 227 0.6× 30 1.3k
Paul W. Ludden United States 48 3.4k 2.1× 3.0k 3.8× 865 1.3× 696 1.1× 1.1k 2.9× 142 6.5k
Robert L. Robson United Kingdom 19 503 0.3× 568 0.7× 228 0.3× 101 0.2× 142 0.4× 26 1.4k
James P. Shapleigh United States 38 248 0.2× 1.5k 2.0× 391 0.6× 193 0.3× 754 1.9× 98 3.7k

Countries citing papers authored by Luis M. Rubio

Since Specialization
Citations

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

Fields of papers citing papers by Luis M. Rubio

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Luis M. Rubio. 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 Luis M. Rubio. The network helps show where Luis M. Rubio may publish in the future.

Co-authorship network of co-authors of Luis M. Rubio

This figure shows the co-authorship network connecting the top 25 collaborators of Luis M. Rubio. A scholar is included among the top collaborators of Luis M. Rubio 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 Luis M. Rubio. Luis M. Rubio 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.
Suess, Daniel L. M., et al.. (2025). Molecular sorting of nitrogenase catalytic cofactors. Journal of Biological Chemistry. 301(3). 108291–108291.
2.
Echávarri‐Erasun, Carlos, et al.. (2024). Iron-molybdenum cofactor synthesis by a thermophilic nitrogenase devoid of the scaffold NifEN. Proceedings of the National Academy of Sciences. 121(46). e2406198121–e2406198121. 3 indexed citations
3.
Campo, Julia S. Martín del, Marcelo Bueno Batista, Florence Mus, et al.. (2022). Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii. Critical Reviews in Biochemistry and Molecular Biology. 57(5-6). 492–538. 25 indexed citations
4.
Baysal, Can, Vicente Medina, Teresa Capell, et al.. (2020). Transit Peptides From Photosynthesis-Related Proteins Mediate Import of a Marker Protein Into Different Plastid Types and Within Different Species. Frontiers in Plant Science. 11. 560701–560701. 8 indexed citations
5.
Buesa, José María, et al.. (2019). Genetic and Biochemical Analysis of the Azotobacter vinelandii Molybdenum Storage Protein. Frontiers in Microbiology. 10. 579–579. 11 indexed citations
6.
Arragain, Simon, et al.. (2017). Diversity and Functional Analysis of the FeMo-Cofactor Maturase NifB. Frontiers in Plant Science. 8. 1947–1947. 18 indexed citations
7.
Burén, Stefan, et al.. (2017). Purification and In Vitro Activity of Mitochondria Targeted Nitrogenase Cofactor Maturase NifB. Frontiers in Plant Science. 8. 1567–1567. 39 indexed citations
8.
Curatti, Leonardo & Luis M. Rubio. (2014). Challenges to develop nitrogen-fixing cereals by direct nif-gene transfer. Plant Science. 225. 130–137. 82 indexed citations
9.
Poza‐Carrión, César, et al.. (2013). Kinetics of nif Gene Expression in a Nitrogen-Fixing Bacterium. Journal of Bacteriology. 196(3). 595–603. 48 indexed citations
10.
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
11.
Hernández, José A., Leonardo Curatti, Constantino P. Aznar, et al.. (2008). Metal trafficking for nitrogen fixation: NifQ donates molybdenum to NifEN/NifH for the biosynthesis of the nitrogenase FeMo-cofactor. Proceedings of the National Academy of Sciences. 105(33). 11679–11684. 53 indexed citations
12.
Zhao, Dehua, Leonardo Curatti, & Luis M. Rubio. (2007). Evidence for nifU and nifS Participation in the Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase. Journal of Biological Chemistry. 282(51). 37016–37025. 46 indexed citations
13.
Curatti, Leonardo, Paul W. Ludden, & Luis M. Rubio. (2006). NifB-dependent in vitro synthesis of the iron–molybdenum cofactor of nitrogenase. Proceedings of the National Academy of Sciences. 103(14). 5297–5301. 83 indexed citations
14.
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
15.
Jeon, Won Bae, Steven W. Singer, Paul W. Ludden, & Luis M. Rubio. (2005). New insights into the mechanism of nickel insertion into carbon monoxide dehydrogenase: analysis of Rhodospirillum rubrum carbon monoxide dehydrogenase variants with substituted ligands to the [Fe3S4] portion of the active-site C-cluster. JBIC Journal of Biological Inorganic Chemistry. 10(8). 903–912. 24 indexed citations
16.
Rubio, Luis M., Steven W. Singer, & Paul W. Ludden. (2004). Purification and Characterization of NafY (Apodinitrogenase γ Subunit) from Azotobacter vinelandii. Journal of Biological Chemistry. 279(19). 19739–19746. 32 indexed citations
17.
Rubio, Luis M., Clive S. Butler, Enrique Flores, et al.. (2004). Tuning a Nitrate Reductase for Function. Journal of Biological Chemistry. 279(31). 32212–32218. 62 indexed citations
18.
Hirasawa, Masakazu, Luis M. Rubio, Enrique Flores, et al.. (2003). Complex formation between ferredoxin and Synechococcus ferredoxin:nitrate oxidoreductase. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1608(2-3). 155–162. 21 indexed citations
19.
Butt, Julea N., et al.. (2002). Enzyme-catalysed nitrate reduction—themes and variations as revealed by protein film voltammetry. Bioelectrochemistry. 56(1-2). 17–18. 8 indexed citations
20.
Rubio, Luis M., Enrique Flores, & Antonia Herrero. (1999). Molybdopterin guanine dinucleotide cofactor in Synechococcus sp. nitrate reductase: identification of mobA and isolation of a putative moeB gene. FEBS Letters. 462(3). 358–362. 20 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

Breakdown of academic impact, for papers by Paul E. Bishop Breakdown of academic impact, for papers by G P Roberts Breakdown of academic impact, for papers by H. Haaker Breakdown of academic impact, for papers by Robert H. Burris Breakdown of academic impact, for papers by Bernard Billoud Breakdown of academic impact, for papers by Yves Jouanneau Breakdown of academic impact, for papers by R L Robson Breakdown of academic impact, for papers by Paul W. Ludden Breakdown of academic impact, for papers by Robert L. Robson Breakdown of academic impact, for papers by James P. Shapleigh
Rankless by CCL
2026