Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Stefan Wahlefeld"'
Autor:
Tobias Werther, Stefan Wahlefeld, Johannes Salewski, Uwe Kuhlmann, Ingo Zebger, Peter Hildebrandt, Holger Dobbek
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
Due to their transient nature, enzyme-substrate complexes are difficult to characterize structurally. Here, the authors capture the reactive reduced form of xenobiotic reductase A bound to its substrate and show that the oxidation state of the flavin
Externí odkaz:
https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d9
Autor:
Catharina J. Kulka-Peschke, Anne-Christine Schulz, Christian Lorent, Yvonne Rippers, Stefan Wahlefeld, Janina Preissler, Claudia Schulz, Charlotte Wiemann, Cornelius C. M. Bernitzky, Chara Karafoulidi-Retsou, Solomon L. D. Wrathall, Barbara Procacci, Hiroaki Matsuura, Gregory M. Greetham, Christian Teutloff, Lars Lauterbach, Yoshiki Higuchi, Masaharu Ishii, Neil T. Hunt, Oliver Lenz, Ingo Zebger, Marius Horch
Publikováno v:
Journal of the American Chemical Society. 144:17022-17032
NAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46bd2c0ed12eca4faae076eabca9ef38
https://doi.org/10.1021/jacs.2c06400
https://doi.org/10.1021/jacs.2c06400
Autor:
Stefan Wahlefeld, Maria Andrea Mroginski, Ingo Zebger, Nicolas Chrysochos, Mohsen Ahmadi, Yvonne Rippers, Carola Schulzke
Publikováno v:
Dalton Transactions. 48:2701-2714
A pair of structurally precise analogues of molybdenum and rhenium complexes, [Et4N]/K2[MoO(prdt)2] and K[ReO(prdt)2] (prdt = pyrazine-2,3-dithiolene), were synthesized. These complexes serve as structural models for the active sites of bacterial mol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee932b76abd3702ba6c49701f6ec367d
https://doi.org/10.1039/c8dt04237c
https://doi.org/10.1039/c8dt04237c
Autor:
Matthias Driess, Tibor Szilvási, Shenglai Yao, Peter Hildebrandt, Stefan Wahlefeld, Marius Horch, Eckhard Bill, Christopher Eberle, Ingo Zebger, Nils Lindenmaier
Publikováno v:
Angewandte Chemie. 129:2243-2247
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb098859035202d9432c462813d7b32b
https://doi.org/10.1002/ange.201611069
https://doi.org/10.1002/ange.201611069
Autor:
Matthias Driess, Ingo Zebger, Stefan Wahlefeld, Marius Horch, Shenglai Yao, Peter Hildebrandt, Nils Lindenmaier, Christopher Eberle, Eckhard Bill, Tibor Szilvási
Publikováno v:
Angewandte Chemie International Edition. 56:2208-2211
To understand the molecular details of O2-tolerant hydrogen cycling by a soluble NAD+-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9891f1784b9bb217b0f278eb8e048bb9
https://doi.org/10.1002/anie.201611069
https://doi.org/10.1002/anie.201611069
Autor:
Ingo Zebger, Stefan Wahlefeld, Oliver Lenz, Marius Horch, Janina Preissler, Christian Teutloff, Stephen P. Cramer, Lars Lauterbach, Christian Lorent
Biocatalysts that mediate the H2-dependent reduction of NAD+ to NADH are attractive from both a fundamental and applied perspective. Here we present the first biochemical and spectroscopic characterization of an NAD+-reducing [NiFe]‑hydrogenase tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79303796d04f3714fbec4ccfe203ebf9
https://refubium.fu-berlin.de/handle/fub188/27684
https://refubium.fu-berlin.de/handle/fub188/27684
Autor:
Janina, Preissler, Stefan, Wahlefeld, Christian, Lorent, Christian, Teutloff, Marius, Horch, Lars, Lauterbach, Stephen P, Cramer, Ingo, Zebger, Oliver, Lenz
Publikováno v:
Biochimica et biophysica acta. Bioenergetics. 1859(1)
Biocatalysts that mediate the H(2)-dependent reduction of NAD(+) to NADH are attractive from both a fundamental and applied perspective. Here we present the first biochemical and spectroscopic characterization of an NAD(+)-reducing [NiFe]-hydrogenase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::785f4107e5dbe526b7bab043ed6ddb61
https://pubmed.ncbi.nlm.nih.gov/28970007
https://pubmed.ncbi.nlm.nih.gov/28970007
Autor:
Nils J, Lindenmaier, Stefan, Wahlefeld, Eckhard, Bill, Tibor, Szilvási, Christopher, Eberle, Shenglai, Yao, Peter, Hildebrandt, Marius, Horch, Ingo, Zebger, Matthias, Driess
Publikováno v:
Angewandte Chemie (International ed. in English). 56(8)
To understand the molecular details of O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b09369b834da29e0d56dd8380047a8a4
https://pubmed.ncbi.nlm.nih.gov/28079958
https://pubmed.ncbi.nlm.nih.gov/28079958
Autor:
Lars Lauterbach, Marius Horch, Katja Karstens, Friedhelm Lendzian, Miriam Grunzel, Stefan Wahlefeld, Oliver Lenz, Ingo Zebger
Publikováno v:
Biochemistry. 54(2)
The soluble NAD(+)-reducing hydrogenase (SH) from Ralstonia eutropha H16 belongs to the O2-tolerant subtype of pyridine nucleotide-dependent [NiFe]-hydrogenases. To identify molecular determinants for the O2 tolerance of this enzyme, we introduced si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770c0f8929b172799d12a92e1df20883
https://pubmed.ncbi.nlm.nih.gov/25517969
https://pubmed.ncbi.nlm.nih.gov/25517969