Zobrazeno 1 - 10
of 46
pro vyhledávání: '"metallocluster"'
Autor:
Pozzi, Cecilia, Ciambellotti, Silvia, Bernacchioni, Caterina, Di Pisa, Flavio, Mangani, Stefano, Turano, Paola
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2017 Mar 01. 114(10), 2580-2585.
Externí odkaz:
https://www.jstor.org/stable/26480072
Autor:
Helena Shomar, Gregory Bokinsky
Publikováno v:
Molecules, Vol 26, Iss 22, p 6930 (2021)
Microbes are routinely engineered to synthesize high-value chemicals from renewable materials through synthetic biology and metabolic engineering. Microbial biosynthesis often relies on expression of heterologous biosynthetic pathways, i.e., enzymes
Externí odkaz:
https://doaj.org/article/021319f26cf64130b3a9067d7617218b
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
Publikováno v:
Molecules: a journal of synthetic organic and natural product chemistry. 26(22)
Microbes are routinely engineered to synthesize high-value chemicals from renewable materials through synthetic biology and metabolic engineering. Microbial biosynthesis often relies on expression of heterologous biosynthetic pathways, i.e., enzymes
Nitrogenases are the only known biological enzyme capable of catalyzing the transformation of dinitrogen (N₂) into ammonia (NH₃). The active site of nitrogenase is comprised of a double-cuboidal iron-sulfur cluster featuring an interstitial carbi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::edba60eb8b0709dbf93ce8aff293a125
Autor:
Christine Cavazza, Marila Alfano
Publikováno v:
Protein Science
Protein Science, Wiley, 2020, 29 (5), pp.1071-1089. ⟨10.1002/pro.3836⟩
Protein Science, 2020, 29 (5), pp.1071-1089. ⟨10.1002/pro.3836⟩
Protein Sci
Protein Science, Wiley, 2020, 29 (5), pp.1071-1089. ⟨10.1002/pro.3836⟩
Protein Science, 2020, 29 (5), pp.1071-1089. ⟨10.1002/pro.3836⟩
Protein Sci
International audience; Nickel enzymes, present in archaea, bacteria, plants and primitive eukaryotes are divided into redox and non-redox enzymes and play key functions in diverse metabolic processes, such as energy metabolism and virulence. They ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd6cf90ef2a9f2e441d82218cee56ee1
https://hal.archives-ouvertes.fr/hal-02476302
https://hal.archives-ouvertes.fr/hal-02476302
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 26(26)
X-ray structures of homopolymeric human L-ferritin and horse spleen ferritin were solved by freezing protein crystals at different time intervals after exposure to a ferric salt and revealed the growth of an octa-nuclear iron cluster on the inner sur
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
Publikováno v:
Encyclopedia of Inorganic and Bioinorganic Chemistry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a2f0309d01584d0c88b0b31ec225694
http://hdl.handle.net/11365/1071988
http://hdl.handle.net/11365/1071988
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