Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Oliver Lampret"'
Autor:
Martin Winkler, Jifu Duan, Andreas Rutz, Christina Felbek, Lisa Scholtysek, Oliver Lampret, Jan Jaenecke, Ulf-Peter Apfel, Gianfranco Gilardi, Francesca Valetti, Vincent Fourmond, Eckhard Hofmann, Christophe Léger, Thomas Happe
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
[FeFe]-hydrogenases catalyze the conversion of protons and electrons to molecular hydrogen, but upon exposure to oxygen, their catalytic cofactor is irreversibly inactivated. Here, the authors determine the crystal structure of hydrogenase CbA5H and
Externí odkaz:
https://doaj.org/article/9c9745d6547b4e9c8c0781318c4c1e61
Autor:
Rieke Haas, Vera Engelbrecht, Oliver Lampret, Shanika Yadav, Ulf‐Peter Apfel, Silke Leimkühler, Thomas Happe
Publikováno v:
ChemBioChem.
Autor:
Oliver Lampret, Martin Winkler, Jifu Duan, Thomas Happe, Fraser A. Armstrong, Eckhard Hofmann
Publikováno v:
Proc Natl Acad Sci U S A
As paradigms for proton-coupled electron transfer in enzymes and benchmarks for a fully renewable H(2) technology, [FeFe]-hydrogenases behave as highly reversible electrocatalysts when immobilized on an electrode, operating in both catalytic directio
Publikováno v:
Physical Chemistry Chemical Physics
Electron transfer processes between proteins are vital in many biological systems. Yet, the role of the solvent in influencing these redox reactions remains largely unknown. In this study, terahertz-time domain spectroscopy (THz-TDS) is used to probe
Autor:
Lisa Scholtysek, Ulf-Peter Apfel, Vincent Fourmond, Christina Felbek, Gianfranco Gilardi, Oliver Lampret, Jan Jaenecke, Francesca Valetti, Jifu Duan, Thomas Happe, Eckhard Hofmann, Andreas Rutz, Martin Winkler, Christophe Léger
Publikováno v:
Nature Communications
Nature Communications, 2021, 12 (1), ⟨10.1038/s41467-020-20861-2⟩
'Nature Communications ', vol: 12, pages: 756-1-756-10 (2021)
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-020-20861-2⟩
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications, 2021, 12 (1), ⟨10.1038/s41467-020-20861-2⟩
'Nature Communications ', vol: 12, pages: 756-1-756-10 (2021)
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-020-20861-2⟩
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
[FeFe]-hydrogenases are efficient H2-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f172a71e483de8388502ba850657f08
https://hal.science/hal-03129104
https://hal.science/hal-03129104
Publikováno v:
Photosynthesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::158017e27b43ad70aceef5a2fb5c4e57
https://doi.org/10.1515/9783110716979-004
https://doi.org/10.1515/9783110716979-004
Autor:
Rieke Haas, Julian Esselborn, Oliver Lampret, Leonie Kertess, Clare F. Megarity, Thomas Happe, Rosalind L. Booth, Martin Winkler, Fraser A. Armstrong, Andreas Rutz, Florian Wittkamp
Publikováno v:
Lampret, O, Esselborn, J, Haas, R, Rutz, A, Booth, R L, Kertess, L, Wittkamp, F, Megarity, C F, Armstrong, F A, Winkler, M & Happe, T 2019, ' The final steps of [FeFe]-hydrogenase maturation ', Proceedings of the National Academy of Sciences of the United States of America, vol. 116, no. 32, pp. 15802-15810 . https://doi.org/10.1073/pnas.1908121116
The active site (H-cluster) of [FeFe]-hydrogenases is a blueprint for the design of a biologically inspired H2-producing catalyst. The maturation process describes the preassembly and uptake of the unique [2FeH] cluster into apo-hydrogenase, which is
Autor:
Hannes Konegger, Florian Wittkamp, Agnieszka Adamska-Venkatesh, Oliver Lampret, Edward J. Reijerse, Wolfgang Lubitz, Martin Winkler, Thomas Happe, Ulf-Peter Apfel, Olaf Rüdiger
Publikováno v:
Journal of the American Chemical Society. 139:18222-18230
The catalytic cofactor of [FeFe]-hydrogenses (H-cluster) is composed of a generic cubane [4Fe-4S]-cluster (4FeH) linked to a binuclear iron–sulfur cluster (2FeH) that has an open coordination site at which the reversible conversion of protons to mo
Autor:
Oliver, Lampret, Agnieszka, Adamska-Venkatesh, Hannes, Konegger, Florian, Wittkamp, Ulf-Peter, Apfel, Edward J, Reijerse, Wolfgang, Lubitz, Olaf, Rüdiger, Thomas, Happe, Martin, Winkler
Publikováno v:
Journal of the American Chemical Society. 139(50)
The catalytic cofactor of [FeFe]-hydrogenses (H-cluster) is composed of a generic cubane [4Fe-4S]-cluster (4Fe