Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Casey Van Stappen"'
Autor:
Sivathmeehan Yogendra, Daniel W. N. Wilson, Anselm W. Hahn, Thomas Weyhermüller, Casey Van Stappen, Patrick Holland, Serena DeBeer
Publikováno v:
Inorganic Chemistry. 62:2663-2671
Autor:
Casey Van Stappen, Yunling Deng, Yiwei Liu, Hirbod Heidari, Jing-Xiang Wang, Yu Zhou, Aaron P. Ledray, Yi Lu
Publikováno v:
Chem Rev
Metalloenzymes catalyze a variety of reactions using a limited number of natural amino acids and metallocofactors. Therefore, the environment beyond the primary coordination sphere must play an important role in both conferring and tuning their pheno
Autor:
Sheetal Sisodiya-Amrute, Casey Van Stappen, Simon Rengshausen, Chenhui Han, Alexandre Sodreau, Claudia Weidenthaler, Simon Tricard, Serena DeBeer, Bruno Chaudret, Alexis Bordet, Walter Leitner
Publikováno v:
Journal of Catalysis
Journal of Catalysis, 2022, 407, pp.141-148. ⟨10.1016/j.jcat.2022.01.030⟩
Journal of catalysis 407, 141-148 (2022). doi:10.1016/j.jcat.2022.01.030
Seminar, Germany
Journal of Catalysis, 2022, 407, pp.141-148. ⟨10.1016/j.jcat.2022.01.030⟩
Journal of catalysis 407, 141-148 (2022). doi:10.1016/j.jcat.2022.01.030
Seminar, Germany
Seminar, Germany; Journal of catalysis 407, 141 - 148 (2022). doi:10.1016/j.jcat.2022.01.030
Bimetallic iron-ruthenium and cobalt-ruthenium nanoparticles with systematic variations in the Fe:Ru and Co:Ru ratios are prepared following an organome
Bimetallic iron-ruthenium and cobalt-ruthenium nanoparticles with systematic variations in the Fe:Ru and Co:Ru ratios are prepared following an organome
Autor:
Casey Van Stappen, Emilio Jiménez-Vicente, Ana Pérez-González, Zhi-Yong Yang, Lance C. Seefeldt, Serena DeBeer, Dennis R. Dean, Laure Decamps
Publikováno v:
Chemistry and Biochemistry Faculty Publications
Reduction of dinitrogen by molybdenum nitrogenase relies on complex metalloclusters: the [8Fe:7S] P-cluster and the [7Fe:9S:Mo:C:homocitrate] FeMo-cofactor. Although both clusters bear topological similarities and require the reductive fusion of [4Fe
Autor:
Aaron P. Ledray, Sudharsan Dwaraknath, Khetpakorn Chakarawet, Madeline R. Sponholtz, Claire Merchen, Casey Van Stappen, Guodong Rao, R. David Britt, Yi Lu
Publikováno v:
Biochemistry, vol 62, iss 2
Biochemistry
Biochemistry
Heme-copper oxidases (HCOs) utilize tyrosine (Tyr) to donate one of the four electrons required for the reduction of O2 to water in biological respiration, while tryptophan (Trp) is speculated to fulfill the same role in cyt bd oxidases. We previousl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8e5b26aaf947744214d0188a93109b8
https://escholarship.org/uc/item/3v23c6ts
https://escholarship.org/uc/item/3v23c6ts
Autor:
Casey Van Stappen, Bardi Benediktsson, Atanu Rana, Aleksandr Chumakov, Yoshitaka Yoda, Dimitrios Bessas, Laure Decamps, Ragnar Bjornsson, Serena DeBeer
Publikováno v:
Faraday Discussions
Faraday Discussions, In press, ⟨10.1039/d2fd00174h⟩
Faraday Discussions, In press, ⟨10.1039/d2fd00174h⟩
International audience; he biological conversion of N-2 to NH3 is accomplished by the nitrogenase family, which is collectively comprised of three closely related but unique metalloenzymes. In the present study, we have employed a combination of the
Autor:
Giorgio Caserta, Sven Hartmann, Casey Van Stappen, Chara Karafoulidi-Retsou, Christian Lorent, Stefan Yelin, Matthias Keck, Janna Schoknecht, Ilya Sergueev, Yoshitaka Yoda, Peter Hildebrandt, Christian Limberg, Serena DeBeer, Ingo Zebger, Stefan Frielingsdorf, Oliver Lenz
Publikováno v:
Nature chemical biology 19(4), 498-506 (2023). doi:10.1038/s41589-022-01226-w
Nature chemical biology 19(4), 498 - 506 (2023). doi:10.1038/s41589-022-01226-w
[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H$_2$ into 2e$^−$ and 2H$^+$ under ambient conditions. Catalysis
[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H$_2$ into 2e$^−$ and 2H$^+$ under ambient conditions. Catalysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1754ea097a8dbf52ea08fcd6e5ce6678
Autor:
Giorgio Caserta, Sven Hartmann, Casey van Stappen, Chara Karafoulidi Retsou, Christian Lorent, Stefan Yelin, Matthias Keck, Janna Schoknecht, Ilya Sergueev, Yoshitaka Yoda, Peter Hildebrandt, Christian Limberg, Serena DeBeer, Ingo Zebger, Stefan Frielingsdorf, Oliver Lenz
[NiFe]-hydrogenases are biotechnologically relevant enzymes catalyzing the reversible splitting of H$_2$ into 2 e$^- $ and 2 H$^+$ under ambient conditions. Catalysis takes place at the heterobimetallic NiFe(CN)$_2$(CO) center, whose multistep biosyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31b5236a53e88544594c0766f74464b1
https://doi.org/10.26434/chemrxiv-2022-jvtgw
https://doi.org/10.26434/chemrxiv-2022-jvtgw
Autor:
Daniel E. DeRosha, Frank Neese, Eckhard Bill, Casey Van Stappen, Serena DeBeer, Brandon Q. Mercado, Vijay Gopal Chilkuri, Patrick L. Holland
Publikováno v:
Nature chemistry
Iron-sulfur clusters are emerging as reactive sites for the reduction of small-molecule substrates. However, the four-coordinate iron sites of typical iron-sulfur clusters rarely react with substrates, implicating three-coordinate iron. This idea is
Autor:
Zhi-Yong Yang, Serena DeBeer, Ruixi Fan, Lance C. Seefeldt, Yisong Guo, Casey Van Stappen, Roman Davydov, Eckhard Bill, Brian M. Hoffman
Publikováno v:
Inorganic Chemistry. 58:12365-12376
Mo nitrogenase (N2ase) utilizes a two-component protein system, the catalytic MoFe and its electron-transfer partner FeP, to reduce atmospheric dinitrogen (N2) to ammonia (NH3). The FeMo cofactor c...