Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Laura, Fradale"'
Autor:
Elizabeth C Wittenborn, Mériem Merrouch, Chie Ueda, Laura Fradale, Christophe Léger, Vincent Fourmond, Maria-Eirini Pandelia, Sébastien Dementin, Catherine L Drennan
Publikováno v:
eLife, Vol 7 (2018)
The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have
Externí odkaz:
https://doaj.org/article/6a9fdef703824e8a8dbe1dc0311b6bd7
Autor:
Cameron D. Fyfe, Noelia Bernardo-García, Laura Fradale, Stéphane Grimaldi, Alain Guillot, Clémence Brewee, Leonard M. G. Chavas, Pierre Legrand, Alhosna Benjdia, Olivier Berteau
Publikováno v:
Nature
Nature, 2022, 602 (7896), pp.336-342. ⟨10.1038/s41586-021-04355-9⟩
Nature, 2022, 602 (7896), pp.336-342. ⟨10.1038/s41586-021-04355-9⟩
By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas1,2. The activity of methyl-coenzyme M reductase is profoundly affected by several unique post-translational m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::467c06b7db558a47cca088e15883638a
https://hal.inrae.fr/hal-03808863/file/2022-Fyfe-Nature.pdf
https://hal.inrae.fr/hal-03808863/file/2022-Fyfe-Nature.pdf
Autor:
Cameron D, Fyfe, Noelia, Bernardo-García, Laura, Fradale, Stéphane, Grimaldi, Alain, Guillot, Clémence, Brewee, Leonard M G, Chavas, Pierre, Legrand, Alhosna, Benjdia, Olivier, Berteau
Publikováno v:
Nature. 602(7896)
By catalysing the microbial formation of methane, methyl-coenzyme M reductase has a central role in the global levels of this greenhouse gas
Autor:
Alhosna Benjdia, Olivier Berteau, Clémence Brewee, Clémence Balty, Alain Guillot, Mylène Boulay, Laura Fradale, Xavier Kubiak
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (40), pp.14512-14525. ⟨10.1074/jbc.RA119.009416⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (40), pp.14512-14525. ⟨10.1074/jbc.RA119.009416⟩
The human microbiota plays a central role in human physiology. This complex ecosystem is a promising but untapped source of bioactive compounds and antibiotics that are critical for its homeostasis. However, we still have a very limited knowledge of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9493d3b8614c38d7894a3a747903854
https://hal.inrae.fr/hal-02868868/document
https://hal.inrae.fr/hal-02868868/document
Autor:
Vincent Fourmond, Matteo Sensi, Melisa del Barrio, Laura Fradale, Christophe Léger, Luca De Gioia, Claudio Greco, Luca Bertini, Maurizio Bruschi
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2018, 140 (16), pp.5485-5492. ⟨10.1021/jacs.8b01414⟩
Journal of the American Chemical Society, American Chemical Society, 2018, 140 (16), pp.5485-5492. ⟨10.1021/jacs.8b01414⟩
Journal of the American Chemical Society, 2018, 140 (16), pp.5485-5492. ⟨10.1021/jacs.8b01414⟩
Journal of the American Chemical Society, American Chemical Society, 2018, 140 (16), pp.5485-5492. ⟨10.1021/jacs.8b01414⟩
International audience; FeFe hydrogenases catalyse H2 oxidation and production using a "H-cluster", where two Fe ions are bound by an aza-dithiolate (adt) ligand. Various hypotheses have been proposed (by us and others) to explain that the enzyme rev
Autor:
Clémence, Balty, Alain, Guillot, Laura, Fradale, Clémence, Brewee, Mylène, Boulay, Xavier, Kubiak, Alhosna, Benjdia, Olivier, Berteau
Publikováno v:
The Journal of Biological Chemistry
The human microbiota plays a central role in human physiology. This complex ecosystem is a promising but untapped source of bioactive compounds and antibiotics that are critical for its homeostasis. However, we still have a very limited knowledge of
Autor:
Christophe Léger, Mériem Merrouch, Chie Ueda, Catherine L. Drennan, Vincent Fourmond, Sébastien Dementin, Laura Fradale, Elizabeth C. Wittenborn, Maria-Eirini Pandelia
Publikováno v:
eLife
eLife, 2018, 7, ⟨10.7554/eLife.39451⟩
eLife, Vol 7 (2018)
eLife, eLife Sciences Publication, 2018, 7, ⟨10.7554/eLife.39451⟩
eLife, 2018, 7, ⟨10.7554/eLife.39451⟩
eLife, Vol 7 (2018)
eLife, eLife Sciences Publication, 2018, 7, ⟨10.7554/eLife.39451⟩
The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO2 to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have
Autor:
Mériem Merrouch, Christophe Léger, Elizabeth C. Wittenborn, Vincent Fourmond, Catherine L. Drennan, Chie Ueda, Maria-Eirini Pandelia, Laura Fradale, Sébastien Dementin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fa89b63c478feda21747bb8d9e7461a
https://doi.org/10.7554/elife.39451.031
https://doi.org/10.7554/elife.39451.031