Evert C. Duin

4.2k total citations
74 papers, 3.0k citations indexed

About

Evert C. Duin is a scholar working on Renewable Energy, Sustainability and the Environment, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Evert C. Duin has authored 74 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Renewable Energy, Sustainability and the Environment, 34 papers in Molecular Biology and 26 papers in Inorganic Chemistry. Recurrent topics in Evert C. Duin's work include Metalloenzymes and iron-sulfur proteins (33 papers), Metal-Catalyzed Oxygenation Mechanisms (23 papers) and Porphyrin Metabolism and Disorders (22 papers). Evert C. Duin is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (33 papers), Metal-Catalyzed Oxygenation Mechanisms (23 papers) and Porphyrin Metabolism and Disorders (22 papers). Evert C. Duin collaborates with scholars based in United States, Germany and Switzerland. Evert C. Duin's co-authors include Simon P. J. Albracht, Rudolf K. Thauer, Felix Mahlert, Reiner Hedderich, William H. Woodruff, Kimberly A. Bagley, Bruce J. Tatarchuk, Alexander Samokhvalov, Bernhard Jaun and Michael K. Johnson and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Chemistry of Materials.

In The Last Decade

Evert C. Duin

73 papers receiving 3.0k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Evert C. Duin United States	32	1.5k	1.1k	797	679	382	74	3.0k
Peter‐Leon Hagedoorn Netherlands	33	646 0.4×	1.5k 1.3×	494 0.6×	570 0.8×	183 0.5×	127	3.2k
Eric M. Shepard United States	28	2.1k 1.4×	1.2k 1.1×	460 0.6×	933 1.4×	315 0.8×	70	3.3k
Joan Broderick United States	44	4.5k 3.1×	2.3k 2.1×	873 1.1×	2.0k 2.9×	532 1.4×	112	6.2k
Steve S.‐F. Yu Taiwan	26	546 0.4×	842 0.7×	935 1.2×	1.2k 1.8×	150 0.4×	90	2.5k
Harry D. Peck United States	31	1.1k 0.8×	1.1k 1.0×	570 0.7×	196 0.3×	229 0.6×	61	2.8k
Bruno Guigliarelli France	34	2.2k 1.5×	753 0.7×	603 0.8×	645 0.9×	607 1.6×	62	3.0k
Eric L. Hegg United States	32	861 0.6×	1.6k 1.5×	527 0.7×	1.0k 1.5×	82 0.2×	78	3.9k
Yue Teng China	26	510 0.4×	945 0.8×	746 0.9×	100 0.1×	403 1.1×	93	2.8k
Sean J. Elliott United States	31	986 0.7×	1.5k 1.3×	444 0.6×	729 1.1×	726 1.9×	90	3.2k
Élisabeth Lojou France	35	1.3k 0.9×	925 0.8×	449 0.6×	178 0.3×	2.4k 6.2×	126	3.8k

Countries citing papers authored by Evert C. Duin

Since Specialization

Citations

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

Fields of papers citing papers by Evert C. Duin

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Evert C. Duin

This figure shows the co-authorship network connecting the top 25 collaborators of Evert C. Duin. A scholar is included among the top collaborators of Evert C. Duin 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 Evert C. Duin. Evert C. Duin 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

Shelton, Emma, Chau-Wen Chou, Nana Shao, et al.. (2025). An Expanded Molecular Model for the Activation of Methyl-Coenzyme M Reductase. Biochemistry. 64(21). 4424–4436.

He, Jianzhou, et al.. (2024). Biochar and surfactant synergistically enhanced PFAS destruction in UV/sulfite system at neutral pH. Chemosphere. 353. 141562–141562. 13 indexed citations

Sutherland‐Smith, Andrew J., Vincenzo Carbone, Linley R. Schofield, et al.. (2024). The crystal structure of methanogen McrD , a methyl‐coenzyme M reductase‐associated protein. FEBS Open Bio. 14(8). 1222–1229. 2 indexed citations

He, Jianzhou, Tae-Sik Oh, Yaniv Olshansky, et al.. (2024). Enhanced sorption and destruction of PFAS by biochar-enabled advanced reduction process. Chemosphere. 363. 142760–142760. 11 indexed citations

Stoian, Sebastian A., Nicholas S. Lees, Bryan T. Cronin, et al.. (2024). The Active-Site [4Fe-4S] Cluster in the Isoprenoid Biosynthesis Enzyme IspH Adopts Unexpected Redox States during Ligand Binding and Catalysis. Journal of the American Chemical Society. 146(6). 3926–3942. 3 indexed citations

Durmic, Z., Evert C. Duin, A. Bannink, et al.. (2024). Feed additives for methane mitigation: Recommendations for identification and selection of bioactive compounds to develop antimethanogenic feed additives. Journal of Dairy Science. 108(1). 302–321. 8 indexed citations

Shao, Nana, Fan Yu, Chau-Wen Chou, et al.. (2022). Expression of divergent methyl/alkyl coenzyme M reductases from uncultured archaea. Communications Biology. 5(1). 1113–1113. 18 indexed citations

Burton, Andricus R., et al.. (2021). Controlling One-Electron vs Two-Electron Pathways in the Multi-Electron Redox Cycle of Nickel Diethyldithiocarbamate. Inorganic Chemistry. 60(17). 13388–13399. 11 indexed citations

Ji, Haodong, Penghui Du, Dongye Zhao, et al.. (2019). 2D/1D graphitic carbon nitride/titanate nanotubes heterostructure for efficient photocatalysis of sulfamethazine under solar light: Catalytic “hot spots” at the rutile–anatase–titanate interfaces. Applied Catalysis B: Environmental. 263. 118357–118357. 278 indexed citations

10.

Islam, Md. Saidul, Evert C. Duin, B. L. Slaten, & G. Mills. (2018). Photoreduction of CHCl₃ in Aqueous SPEEK/HCO₂^– Solutions Involving Free Radicals. The Journal of Physical Chemistry A. 122(36). 7118–7130. 2 indexed citations

11.

Duin, Evert C., et al.. (2011). Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis. Methods in enzymology on CD-ROM/Methods in enzymology. 494. 159–187. 12 indexed citations

12.

Hernández, Heather L., et al.. (2006). Possible direct involvement of the active‐site [4Fe–4S] cluster of the GcpE enzyme from Thermus thermophilus in the conversion of MEcPP. FEBS Letters. 581(2). 279–283. 25 indexed citations

13.

Goenrich, Meike, Evert C. Duin, Felix Mahlert, & Rudolf K. Thauer. (2005). Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B. JBIC Journal of Biological Inorganic Chemistry. 10(4). 333–342. 47 indexed citations

14.

Mander, Gerd J., et al.. (2003). Physiological role of the F 420 -non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis. Archives of Microbiology. 180(3). 194–203. 70 indexed citations

15.

Mahlert, Felix, Wolfgang Grabarse, Jörg Kahnt, Rudolf K. Thauer, & Evert C. Duin. (2002). The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states (vol 7, pg 101, 2002). JBIC Journal of Biological Inorganic Chemistry. 7(3). 351–351. 1 indexed citations

16.

Kollas, Ann‐Kristin, Evert C. Duin, Matthias Eberl, et al.. (2002). Functional characterization of GcpE, an essential enzyme of the non‐mevalonate pathway of isoprenoid biosynthesis. FEBS Letters. 532(3). 432–436. 96 indexed citations

17.

Altincicek, Boran, Evert C. Duin, Armin Reichenberg, et al.. (2002). LytB protein catalyzes the terminal step of the 2‐C‐methyl‐D‐erythritol‐4‐phosphate pathway of isoprenoid biosynthesis. FEBS Letters. 532(3). 437–440. 129 indexed citations

18.

Mahlert, Felix, Carsten Bauer, Bernhard Jaun, Rudolf K. Thauer, & Evert C. Duin. (2002). The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2. JBIC Journal of Biological Inorganic Chemistry. 7(4-5). 500–513. 42 indexed citations

19.

Duin, Evert C., et al.. (2001). A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. European Journal of Biochemistry. 268(9). 2566–2577. 41 indexed citations

20.

Bagley, Kimberly A., Carla J. Van Garderen, Min Chen, et al.. (1994). Infrared Studies on the Interaction of Carbon Monoxide with Divalent Nickel in Hydrogenase from Chromatium vinosum. Biochemistry. 33(31). 9229–9236. 122 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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