Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Benjamin R. Duffus"'
Publikováno v:
Inorganics, Vol 12, Iss 3, p 67 (2024)
All kingdoms of life have more than 150 different forms of RNA alterations, with tRNA accounting for around 80% of them. These chemical alterations include, among others, methylation, sulfuration, hydroxylation, and acetylation. These changes are nec
Externí odkaz:
https://doaj.org/article/d9aa81fc72a74020bb5ad280b51da762
Autor:
Christin Radon, Gerd Mittelstädt, Benjamin R. Duffus, Jörg Bürger, Tobias Hartmann, Thorsten Mielke, Christian Teutloff, Silke Leimkühler, Petra Wendler
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Rhodobacter capsulatus NAD+ dependent formate dehydrogenase (RcFDH) is a molybdoenzyme that catalyses the reversible oxidation of formate to carbon dioxide, and is of interest for biotechnological applications. Here the authors present the cryo-EM st
Externí odkaz:
https://doaj.org/article/ee6fb5dae1e445018b0579d644893722
Autor:
Sven T. Stripp, Benjamin R. Duffus, Vincent Fourmond, Christophe Léger, Silke Leimkühler, Shun Hirota, Yilin Hu, Andrew Jasniewski, Hideaki Ogata, Markus W. Ribbe
Publikováno v:
Chemical Reviews
Chemical Reviews, 2022, 122 (14), pp.11900-11973. ⟨10.1021/acs.chemrev.1c00914⟩
Chemical Reviews, 2022, 122 (14), pp.11900-11973. ⟨10.1021/acs.chemrev.1c00914⟩
International audience; Gases like H2, N2, CO2, and CO are increasingly recognized as critical feedstock in “green” energy conversion and as sources of nitrogen and carbon for the agricultural and chemical sectors. However, the industrial transfo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c3c54c513dccc40e27763d4f02c2413
https://doi.org/10.1021/acs.chemrev.1c00914
https://doi.org/10.1021/acs.chemrev.1c00914
Autor:
Konstantin Laun, Benjamin R. Duffus, Hemant Kumar, Jean‐Pierre H. Oudsen, Chara Karafoulidi‐Retsou, Armel Tadjoung Waffo, Peter Hildebrandt, Khoa Hoang Ly, Silke Leimkühler, Sagie Katz, Ingo Zebger
Publikováno v:
ChemCatChem. 14
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4564440b3d26c3770473ac533c0965d
https://doi.org/10.1002/cctc.202201067
https://doi.org/10.1002/cctc.202201067
Autor:
Elizabeth C. McDaniel, Jeremiah N. Betz, William E. Broderick, Joan B. Broderick, Adrien Pagnier, Eric M. Shepard, John W. Peters, Amanda S. Byer, Stella Impano, Amanda Galambas, Hope Watts, Kaitlin S. Duschene, Benjamin R. Duffus, Shawn E. McGlynn
Publikováno v:
Dalton Transactions. 50:10405-10422
The organometallic H-cluster of the [FeFe]-hydrogenase consists of a [4Fe-4S] cubane bridged via a cysteinyl thiolate to a 2Fe subcluster ([2Fe]H) containing CO, CN-, and dithiomethylamine (DTMA) ligands. The H-cluster is synthesized by three dedicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3bcff9b8c51cdf25076b11b64769e81
https://doi.org/10.1039/d1dt01359a
https://doi.org/10.1039/d1dt01359a
Autor:
Eric M, Shepard, Stella, Impano, Benjamin R, Duffus, Adrien, Pagnier, Kaitlin S, Duschene, Jeremiah N, Betz, Amanda S, Byer, Amanda, Galambas, Elizabeth C, McDaniel, Hope, Watts, Shawn E, McGlynn, John W, Peters, William E, Broderick, Joan B, Broderick
Publikováno v:
Dalton Trans
The organometallic H-cluster of the [FeFe]-hydrogenase consists of a [4Fe–4S] cubane bridged via a cysteinyl thiolate to a 2Fe subcluster ([2Fe](H)) containing CO, CN(−), and dithiomethylamine (DTMA) ligands. The H-cluster is synthesized by three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b1bae996cd2b917f0d074847f2875cd2
https://pubmed.ncbi.nlm.nih.gov/34240096
https://pubmed.ncbi.nlm.nih.gov/34240096
Autor:
Silke Leimkühler, Benjamin R. Duffus, Holger Dau, Peer Schrapers, Michael Haumann, Nils Schuth, Stefan Mebs
Publikováno v:
Inorganic Chemistry. 59:214-225
Formate dehydrogenase (FDH) enzymes are versatile catalysts for CO2 conversion. The FDH from Rhodobacter capsulatus contains a molybdenum cofactor with the dithiolene functions of two pyranopterin guanine dinucleotide molecules, a conserved cysteine,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f2fbce0b326e05cbe521a6b7dd3a02c
https://doi.org/10.1021/acs.inorgchem.9b01613
https://doi.org/10.1021/acs.inorgchem.9b01613
Autor:
Silke Leimkühler, Petra Wendler, Benjamin R. Duffus, Jörg Bürger, Thorsten Mielke, Tobias Hartmann, Christian Teutloff, Christin Radon, Gerd Mittelstädt
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b62ab6f961453be82b899d84cabd69
https://hdl.handle.net/21.11116/0000-0006-4E44-721.11116/0000-0006-4E46-5
https://hdl.handle.net/21.11116/0000-0006-4E44-721.11116/0000-0006-4E46-5
Autor:
Benjamin R, Duffus, Peer, Schrapers, Nils, Schuth, Stefan, Mebs, Holger, Dau, Silke, Leimkühler, Michael, Haumann
Publikováno v:
Inorganic chemistry. 59(1)
Formate dehydrogenase (FDH) enzymes are versatile catalysts for CO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c7602ea813c7adfd72d4536a0f4029c0
https://pubmed.ncbi.nlm.nih.gov/31814403
https://pubmed.ncbi.nlm.nih.gov/31814403
Autor:
Stefan Reschke, Peer Schrapers, Benjamin R. Duffus, Michael Haumann, Stefan Mebs, Christian Teutloff, Silke Leimkühler, Holger Dau
The oxidoreductase YdhV in Escherichia coli has been predicted to belong to the family of molybdenum/tungsten cofactor (Moco/Wco)-containing enzymes. In this study, we characterized the YdhV protein in detail, which shares amino acid sequence homolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e080ac35bba8db6d737ea4f5d8ba0f5
https://doi.org/10.17169/refubium-26835
https://doi.org/10.17169/refubium-26835