Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Christina S. Müller"'
Autor:
Sylvain Gervason, Djabir Larkem, Amir Ben Mansour, Thomas Botzanowski, Christina S. Müller, Ludovic Pecqueur, Gwenaelle Le Pavec, Agnès Delaunay-Moisan, Omar Brun, Jordi Agramunt, Anna Grandas, Marc Fontecave, Volker Schünemann, Sarah Cianférani, Christina Sizun, Michel B. Tolédano, Benoit D’Autréaux
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The mechanism of iron-sulfur (Fe-S) cluster biosynthesis is not fully understood. Here, the authors develop a physiologically relevant in vitro model of Fe-S cluster assembly, allowing them to elucidate the sequence of Fe-S cluster synthesis along wi
Externí odkaz:
https://doaj.org/article/0caed53885d74e1e9349cdbf6fc819af
Autor:
Max Willistein, Dominique F. Bechtel, Christina S. Müller, Ulrike Demmer, Larissa Heimann, Kanwal Kayastha, Volker Schünemann, Antonio J. Pierik, G. Matthias Ullmann, Ulrich Ermler, Matthias Boll
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
The reduction of 2-naphtoyl-CoA to 5,6 dihydro-2-naphtoyl-CoA by 2-naphtoyl-CoA reductase is below the negative redox limit usually encountered in biological hydride transfer. Here, via X-ray crystallography and spectroscopic analysis, the authors el
Externí odkaz:
https://doaj.org/article/5384fcc9585141cc8574aa70b0d76cdc
Autor:
Simona Riedel, Beata Siemiatkowska, Mutsumi Watanabe, Christina S. Müller, Volker Schünemann, Rainer Hoefgen, Silke Leimkühler
Publikováno v:
Frontiers in Microbiology, Vol 10 (2019)
The mitochondrial ATP-binding cassette (ABC) transporters ABCB7 in humans, Atm1 in yeast and ATM3 in plants, are highly conserved in their overall architecture and particularly in their glutathione binding pocket located within the transmembrane span
Externí odkaz:
https://doaj.org/article/fa5872c6323a4840b34df1ab037124bf
Autor:
Joachim Heberle, Volker Schünemann, Sven T. Stripp, Antonio J. Pierik, Lorenz Adrian, Ramona Schlesinger, Jonathan Oltmanns, Basem Soboh, D. Ehrenberg, Christina S. Müller
Publikováno v:
Biochemical Journal
The [4Fe-4S] cluster containing scaffold complex HypCD is the central construction site for the assembly of the [Fe](CN)2CO cofactor precursor of [NiFe]-hydrogenase. While the importance of the HypCD complex is well established, not much is known abo
Autor:
Marc Walker, Juliusz A. Wolny, Christina S. Müller, Jane M. Donnelly, Peter B. O’Connor, Frederik Lermyte, Ben Breeze, Peter J. Sadler, Volker Schünemann, Joanna F. Collingwood, Russell J. Needham
Publikováno v:
Chemical Communications. 57:69-72
The stable complex [bis(toluene-3,4-dithiolato)copper(iii)][NEt3H] has been synthesised and characterised as a square-planar Cu(iii) complex by X-ray photoelectron spectroscopy, cyclic voltammetry and DFT calculations. Intriguingly, when fragmented i
Autor:
Marie Bergner, Christine E. Schiewer, Juliusz A. Wolny, Franc Meyer, Christina S. Müller, Volker Schünemann, Sebastian Dechert
Publikováno v:
Inorganic Chemistry. 58:769-784
The nitrosylation of biological Fe/S clusters to give protein-bound dinitrosyl iron complexes (DNICs) is physiologically important. Biomimetic studies on the reaction of synthetic [2Fe–2S] clusters with NO have so far been limited to diferric model
Autor:
Lena Scherthan, Christina S. Müller, Volker Schünemann, Hans-Christian Wille, Ralf Röhlsberger, Ilya Sergueev, Olaf Leupold, Juliusz A. Wolny, K. Jenni, Marcus Herlitschke, Sakshath Sadashivaiah, Andreas Omlor
Publikováno v:
The journal of physical chemistry letters. 12(12)
Phonon modes play a vital role in the cooperative phenomenon of light-induced spin transitions in spin crossover (SCO) molecular complexes. Although the cooperative vibrations, which occur over several hundreds of picoseconds to nanoseconds after pho
Autor:
Christina S. Müller, Susanne Schipper, Ricardo Nowack, Laura Magdalena Jordt, Carsten Berndt, Oliver Handorf, Volker Schünemann, Claudia Urbainsky, Yana Bodnar, Christopher Horst Lillig, Carola Schulzke, Jean-Marc Moulis, Eva-Maria Hanschmann
Thioredoxins (Trxs) provide electrons to essential cellular processes such as DNA synthesis. Here, we characterize human and murine Trx1 as new iron-sulfur proteins. The [2Fe-2S] cluster is complexed using cysteinyl side chains 32 and 73 in a dimeric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0428f96960ca966bf8acd1b12426d352
https://doi.org/10.1101/2020.08.04.235721
https://doi.org/10.1101/2020.08.04.235721
Correction to: Characterization of Mycobacterium tuberculosis ferredoxin with Mössbauer spectroscopy
Autor:
Antonio J. Pierik, Volker Schünemann, Hendrik Auerbach, Christina S. Müller, Juliusz A. Wolny, Dominique F. Bechtel
Publikováno v:
Hyperfine Interactions. 241
The article was published with erroneous values in Table 1. Please find in this document the correct version of Table 1 that should be regarded as the final version by the reader
Autor:
Sergej Lauk, Hans-Christian Wille, Christina S. Müller, Helmut Sitzmann, Olaf Leupold, Tim Hochdörffer, Volker Schünemann, Juliusz A. Wolny, René Steinbrügge, Ilya Sergeev, Andreas Omlor, Hendrik Auerbach, Lena Scherthan
Publikováno v:
Hyperfine Interactions. 241
The vibronic properties of two dimeric iron (II) high-spin complexes [5CpFeX]2 (5Cp = Pentaisopropyl-cyclopentadienyl, X = OH-(1), Br-(2)) have been studied using nuclear inelastic scattering (NIS). In order to assign the experimentally observed band