Lars Lauterbach

1.7k total citations
55 papers, 1.2k citations indexed

About

Lars Lauterbach is a scholar working on Renewable Energy, Sustainability and the Environment, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Lars Lauterbach has authored 55 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Renewable Energy, Sustainability and the Environment, 26 papers in Molecular Biology and 9 papers in Inorganic Chemistry. Recurrent topics in Lars Lauterbach's work include Metalloenzymes and iron-sulfur proteins (32 papers), Electrocatalysts for Energy Conversion (15 papers) and Enzyme Catalysis and Immobilization (14 papers). Lars Lauterbach is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (32 papers), Electrocatalysts for Energy Conversion (15 papers) and Enzyme Catalysis and Immobilization (14 papers). Lars Lauterbach collaborates with scholars based in Germany, United Kingdom and United States. Lars Lauterbach's co-authors include Oliver Lenz, Kylie A. Vincent, Ingo Zebger, Marius Horch, Holly A. Reeve, Peter Hildebrandt, Stefan Frielingsdorf, Marion B. Ansorge‐Schumacher, Bettina M. Nestl and Stephen P. Cramer and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Lars Lauterbach

54 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lars Lauterbach Germany 21 700 455 211 191 188 55 1.2k
Benjamin R. Duffus Germany 13 964 1.4× 496 1.1× 35 0.2× 189 1.0× 121 0.6× 21 1.3k
B.H. Huynh United States 19 903 1.3× 462 1.0× 104 0.5× 427 2.2× 109 0.6× 26 1.5k
Masaki Nojiri Japan 17 195 0.3× 652 1.4× 46 0.2× 215 1.1× 73 0.4× 34 1.1k
Vincent C.‐C. Wang Taiwan 16 452 0.6× 257 0.6× 39 0.2× 325 1.7× 125 0.7× 22 1.1k
Martin T. Stiebritz Switzerland 18 646 0.9× 177 0.4× 28 0.1× 193 1.0× 102 0.5× 39 848
Xiaona Li China 18 486 0.7× 163 0.4× 161 0.8× 318 1.7× 378 2.0× 33 1.2k
Nimesh Khadka United States 15 1.3k 1.8× 187 0.4× 32 0.2× 571 3.0× 132 0.7× 18 1.6k
Clare F. Megarity United Kingdom 19 299 0.4× 353 0.8× 55 0.3× 94 0.5× 322 1.7× 30 779
J. Rawlings United States 15 502 0.7× 354 0.8× 34 0.2× 213 1.1× 63 0.3× 34 990
J.W. van der Zwaan Netherlands 14 582 0.8× 211 0.5× 49 0.2× 229 1.2× 89 0.5× 16 799

Countries citing papers authored by Lars Lauterbach

Since Specialization
Citations

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

Fields of papers citing papers by Lars Lauterbach

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lars Lauterbach

This figure shows the co-authorship network connecting the top 25 collaborators of Lars Lauterbach. A scholar is included among the top collaborators of Lars Lauterbach 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 Lars Lauterbach. Lars Lauterbach 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.
Till, J. E., Jörg Toepel, Jens Appel, et al.. (2025). Engineering O 2 -Tolerant Chimeric Hydrogenases Optimized for Ferredoxin Coupling in Synechocystis sp. PCC 6803. ACS Synthetic Biology. 14(11). 4478–4495. 1 indexed citations
2.
González, I., Nathalie Gorret, Lars Lauterbach, & Stéphane Guillouet. (2025). Glycerol-supplemented medium promotes transition of Cupriavidus necator from heterotrophic to lithoautotrophic growth. Biotechnology Letters. 48(1). 3–3.
3.
Guillouet, Stéphane, et al.. (2025). Isopropanol production from carbon dioxide by Cupriavidus necator using a zero-gap cell with culture broth as catholyte. iScience. 28(8). 113018–113018. 1 indexed citations
4.
Lorent, Christian, et al.. (2024). Insights into electron transfer and bifurcation of the Synechocystis sp. PCC6803 hydrogenase reductase module. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1866(1). 149508–149508. 2 indexed citations
5.
Calabrese, Donato, Paul R. F. Cordero, Dörte Rother, et al.. (2024). H2-driven biocatalysis for flavin-dependent ene-reduction in a continuous closed-loop flow system utilizing H2 from water electrolysis. Communications Chemistry. 7(1). 200–200. 5 indexed citations
6.
Peng, Yong, Nils Rockstroh, Stephan Bartling, et al.. (2024). State‐of‐the‐Art Light‐Driven Hydrogen Generation from Formic Acid and Utilization in Enzymatic Hydrogenations. ChemSusChem. 18(4). e202401811–e202401811. 2 indexed citations
7.
Rowbotham, Jack S., Miguel A. Ramirez, Gogulan Karunanithy, et al.. (2023). Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR. Chemical Science. 14(43). 12160–12165. 5 indexed citations
8.
Lauterbach, Lars, et al.. (2023). Toward a synthetic hydrogen sensor in cyanobacteria: Functional production of an oxygen-tolerant regulatory hydrogenase in Synechocystis sp. PCC 6803. Frontiers in Microbiology. 14. 1122078–1122078. 6 indexed citations
9.
Reeve, Holly A., Lars Lauterbach, Oliver Lenz, et al.. (2022). A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H. Chemical Communications. 58(75). 10540–10543. 10 indexed citations
10.
Caserta, Giorgio, Vladimir Pelmenschikov, Christian Lorent, et al.. (2020). Hydroxy-bridged resting states of a [NiFe]-hydrogenase unraveled by cryogenic vibrational spectroscopy and DFT computations. Chemical Science. 12(6). 2189–2197. 22 indexed citations
11.
12.
Willot, Sébastien J.‐P., et al.. (2020). H 2 as a fuel for flavin- and H 2 O 2 -dependent biocatalytic reactions. Chemical Communications. 56(67). 9667–9670. 24 indexed citations
13.
Frielingsdorf, Stefan, Lars Lauterbach, Giovanni Bistoni, et al.. (2019). Formyltetrahydrofolate Decarbonylase Synthesizes the Active Site CO Ligand of O 2 -Tolerant [NiFe] Hydrogenase. Journal of the American Chemical Society. 142(3). 1457–1464. 20 indexed citations
14.
Lauterbach, Lars, et al.. (2019). Cascade Biotransformation to Access 3‐Methylpiperidine in Whole Cells. ChemCatChem. 11(23). 5738–5742. 8 indexed citations
15.
Nestl, Bettina M., et al.. (2019). Synthesis ofN-heterocycles from diaminesviaH2-driven NADPH recycling in the presence of O2. Green Chemistry. 21(6). 1396–1400. 26 indexed citations
16.
Lenz, Oliver, Lars Lauterbach, & Stefan Frielingsdorf. (2018). O2-tolerant [NiFe]-hydrogenases of Ralstonia eutropha H16: Physiology, molecular biology, purification, and biochemical analysis. Methods in enzymology on CD-ROM/Methods in enzymology. 613. 117–151. 46 indexed citations
17.
Lauterbach, Lars & Oliver Lenz. (2018). How to make the reducing power of H2 available for in vivo biosyntheses and biotransformations. Current Opinion in Chemical Biology. 49. 91–96. 24 indexed citations
18.
Lorent, Christian, Christian Teutloff, Marius Horch, et al.. (2017). Enzymatic and spectroscopic properties of a thermostable [NiFe]‑hydrogenase performing H2-driven NAD+-reduction in the presence of O2. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859(1). 8–18. 20 indexed citations
19.
Reeve, Holly A., Lars Lauterbach, Philip A. Ash, Oliver Lenz, & Kylie A. Vincent. (2011). A modular system for regeneration of NADcofactors using graphite particles modified with hydrogenase and diaphorase moieties. Chemical Communications. 48(10). 1589–1591. 49 indexed citations
20.
Lauterbach, Lars, et al.. (2011). Catalytic Properties of the Isolated Diaphorase Fragment of the NAD+-Reducing [NiFe]-Hydrogenase from Ralstonia eutropha. PLoS ONE. 6(10). e25939–e25939. 48 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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