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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Proton Transfer Mechanisms in Bimetallic Hydrogenases
Hulin Tai, Shun Hirota, Sven T. Stripp
Accounts of Chemical Research (2020) Vol. 54, Iss. 1, pp. 232-241
Open Access | Times Cited: 56

Showing 1-25 of 56 citing articles:

Metalloporphyrins as Catalytic Models for Studying Hydrogen and Oxygen Evolution and Oxygen Reduction Reactions
Xialiang Li, Haitao Lei, Lisi Xie, et al.
Accounts of Chemical Research (2022) Vol. 55, Iss. 6, pp. 878-892
Closed Access | Times Cited: 244
Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, et al.
Chemical Reviews (2022) Vol. 122, Iss. 14, pp. 11900-11973
Open Access | Times Cited: 128
Hydrogen-oxidizing bacteria and their applications in resource recovery and pollutant removal
Lin Lin, Haining Huang, Xin Zhang, et al.
The Science of The Total Environment (2022) Vol. 835, pp. 155559-155559
Closed Access | Times Cited: 46
Demonstrating the Electron–Proton-Transfer Mechanism of Aqueous Phase 4-Nitrophenol Hydrogenation Using Unbiased Electrochemical Cells
Hua An, Geng Sun, Max J. Hülsey, et al.
ACS Catalysis (2022) Vol. 12, Iss. 24, pp. 15021-15027
Closed Access | Times Cited: 37
Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli
Ralf Steinhilper, Gabriele Höff, Johann Heider, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 36
Long-range electron proton coupling in respiratory complex I — insights from molecular simulations of the quinone chamber and antiporter-like subunits
Amina Djurabekova, Jonathan Lasham, Oleksii Zdorevskyi, et al.
Biochemical Journal (2024) Vol. 481, Iss. 7, pp. 499-514
Closed Access | Times Cited: 7
Improving Active Site Local Proton Transfer in Porous Organic Polymers for Boosted Oxygen Electrocatalysis
Qian Zhao, Qingxin Zhang, Yuhan Xu, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 47
Closed Access | Times Cited: 6
Functional Dynamics of an Ancient Membrane-Bound Hydrogenase
Max E. Mühlbauer, Ana P. Gámiz‐Hernández, Ville R. I. Kaila
Journal of the American Chemical Society (2021) Vol. 143, Iss. 49, pp. 20873-20883
Open Access | Times Cited: 35
Combining metal–metal cooperativity, metal–ligand cooperativity and chemical non-innocence in diiron carbonyl complexes
Cody B. van Beek, Nicolaas P. van Leest, Martin Lutz, et al.
Chemical Science (2022) Vol. 13, Iss. 7, pp. 2094-2104
Open Access | Times Cited: 24
Replacing a Cysteine Ligand by Selenocysteine in a [NiFe]-Hydrogenase Unlocks Hydrogen Production Activity and Addresses the Role of Concerted Proton-Coupled Electron Transfer in Electrocatalytic Reversibility
Rhiannon M. Evans, Natalie Krahn, Joshua M. Weiss, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 25, pp. 16971-16976
Open Access | Times Cited: 5
Unusual structures and unknown roles of FeS clusters in metalloenzymes seen from a resonance Raman spectroscopic perspective
Giorgio Caserta, Lidia Zuccarello, Catarina Barbosa, et al.
Coordination Chemistry Reviews (2021) Vol. 452, pp. 214287-214287
Open Access | Times Cited: 31
In Situ Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes
Sven T. Stripp
ACS Catalysis (2021) Vol. 11, Iss. 13, pp. 7845-7862
Closed Access | Times Cited: 29
Bioinspired Molecular Electrocatalysts for H2Production: Chemical Strategies
Lili Sun, Carole Duboc, Kaiji Shen
ACS Catalysis (2022) Vol. 12, Iss. 15, pp. 9159-9170
Closed Access | Times Cited: 20
Diiron azadithiolate models with bulky bridgehead moiety: Synthesis, structure and electrochemistry
Xin‐Ping Gao, Shun‐Xi Li, Kui Hu, et al.
Journal of Molecular Structure (2024) Vol. 1306, pp. 137881-137881
Closed Access | Times Cited: 4
Biogenic palladium nanoparticles for wastewater treatment: Formation, applications, limitations, and future directions
Xiaodi Li, Lin Yang, Jingzhou Zhou, et al.
Journal of Water Process Engineering (2024) Vol. 64, pp. 105641-105641
Closed Access | Times Cited: 4
Electrocatalytic CO2 reduction by a cobalt porphyrin mini-enzyme
Alison A. Salamatian, Jose L. Alvarez-Hernandez, K. Ramesh, et al.
Chemical Science (2025)
Open Access
The unusual formaldehyde-induced activation of [NiFe]-hydrogenase: Implications from protein film electrochemistry and infrared spectroscopy
Lei Wan, Yanxin Gao, Serena DeBeer, et al.
Bioelectrochemistry (2025), pp. 108974-108974
Closed Access
Ab initio deep neural network simulations reveal that carbonic acid dissociation is dominated by minority cis-trans conformers
Yanling Zhao, Feifei Tian, Zhaoru Sun
Science Advances (2025) Vol. 11, Iss. 19
Closed Access
A personal account on 25 years of scientific literature on [FeFe]-hydrogenase
Jason W. Sidabras, Sven T. Stripp
JBIC Journal of Biological Inorganic Chemistry (2023) Vol. 28, Iss. 4, pp. 355-378
Closed Access | Times Cited: 9
Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase
Princess R. Cabotaje, Kaija Walter, Afridi Zamader, et al.
ACS Catalysis (2023) Vol. 13, Iss. 15, pp. 10435-10446
Open Access | Times Cited: 9
Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima
Nipa Chongdar, Patricia Rodríguez‐Maciá, Edward J. Reijerse, et al.
Chemical Science (2023) Vol. 14, Iss. 13, pp. 3682-3692
Open Access | Times Cited: 8
Metatranscriptomic insights into the microbial electrosynthesis of acetate by Fe2+/Ni2+ addition
Jie Zhang, He Liu, Yan Zhang, et al.
World Journal of Microbiology and Biotechnology (2023) Vol. 39, Iss. 5
Open Access | Times Cited: 8
Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
Christian Lorent, Vladimir Pelmenschikov, Stefan Frielingsdorf, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 29, pp. 15854-15862
Open Access | Times Cited: 19
Site-selective protonation of the one-electron reduced cofactor in [FeFe]-hydrogenase
Konstantin Laun, Iuliia Baranova, Jifu Duan, et al.
Dalton Transactions (2021) Vol. 50, Iss. 10, pp. 3641-3650
Open Access | Times Cited: 17
Non-contact biomimetic mechanism for selective hydrogenation of nitroaromatics on heterogeneous metal nanocatalysts
Wenting Zhou, Laiyang Li, Ruixuan Qin, et al.
Science China Chemistry (2022) Vol. 65, Iss. 4, pp. 726-732
Closed Access | Times Cited: 12
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