Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Elizabeth C Wittenborn"'
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:
eLife, Vol 5 (2016)
The metallocofactor involved in fixing nitrogen is not a rigid scaffold, as was previously thought.
Externí odkaz:
https://doaj.org/article/01db5a3bc2a644faaa410dc1e0187c61
Autor:
Elizabeth C. Wittenborn, William C. Thomas, Kimberly A. Houghton, Erika S. Wirachman, Yang Wu, Michael A. Marletta
Publikováno v:
Biochemistry. 62:1568-1576
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::165ecb3fccd58bbc48198a257cee6f8f
https://doi.org/10.1021/acs.biochem.3c00052
https://doi.org/10.1021/acs.biochem.3c00052
Autor:
Christopher M. Lemon, Amos J. Nissley, Naomi R. Latorraca, Elizabeth C. Wittenborn, Michael A. Marletta
Publikováno v:
RSC Chemical Biology. 3:571-581
Replacing the native porphyrin cofactor in haem proteins has led to the development of novel designer proteins for a variety of applications. In most cases, haem analogues bind in a way that is comparable to the iron porphyrin, but this is not necess
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97cd4559d88c59e7270ce0e65b9ae581
https://doi.org/10.1039/d2cb00004k
https://doi.org/10.1039/d2cb00004k
Autor:
Mériem Merrouch, Catherine L. Drennan, Vincent Fourmond, Elizabeth C. Wittenborn, Steven E. Cohen, Sébastien Dementin, Christophe Léger
Publikováno v:
J Biol Chem
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
Journal of Biological Chemistry, In press, pp.jbc.RA119.009610. ⟨10.1074/jbc.RA119.009610⟩
The nickel-dependent carbon monoxide dehydrogenase (CODH) employs a unique heterometallic nickel–iron–sulfur cluster, termed the C-cluster, to catalyze the interconversion of CO and CO(2). Like other complex metalloenzymes, CODH requires dedicate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9b47de955c61cc33bdfa835481fd473
https://doi.org/10.1074/jbc.ra119.009610
https://doi.org/10.1074/jbc.ra119.009610
Publikováno v:
International journal of molecular sciences, vol 22, iss 11
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 5439, p 5439 (2021)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 5439, p 5439 (2021)
The enzyme soluble guanylate cyclase (sGC) is the prototypical nitric oxide (NO) receptor in humans and other higher eukaryotes and is responsible for transducing the initial NO signal to the secondary messenger cyclic guanosine monophosphate (cGMP).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fcb2871e81af90f23f728456b72e92c
https://escholarship.org/uc/item/1tg7k3j7
https://escholarship.org/uc/item/1tg7k3j7
Autor:
Catherine L. Drennan, Chloé Guendon, Martino Benvenuti, Mériem Merrouch, Vincent Fourmond, Christophe Léger, Sébastien Dementin, Elizabeth C. Wittenborn
Publikováno v:
ACS Catalysis
ACS Catalysis, American Chemical Society, 2020, 10 (13), pp.7328-7335. ⟨10.1021/acscatal.0c00934⟩
ACS Catalysis, 2020, 10 (13), pp.7328-7335. ⟨10.1021/acscatal.0c00934⟩
ACS Catalysis, American Chemical Society, 2020, 10 (13), pp.7328-7335. ⟨10.1021/acscatal.0c00934⟩
ACS Catalysis, 2020, 10 (13), pp.7328-7335. ⟨10.1021/acscatal.0c00934⟩
International audience; Ni-Fe CO-dehydrogenases (CODHs) catalyze the conversion between CO and CO 2 using a chain of Fe-S clusters to mediate long-range electron transfer. One of these clusters, the D-cluster, is surface-exposed and serves to transfe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d693b0f5d79af49629d5df8160aec080
https://hal.archives-ouvertes.fr/hal-02936282/document
https://hal.archives-ouvertes.fr/hal-02936282/document
Autor:
Catherine L. Drennan, Edward J. Brignole, Elizabeth C. Wittenborn, Samuel Thompson, Mehmet Can, Stephen W. Ragsdale, Steven E. Cohen
Publikováno v:
Structure
The nickel-iron-sulfur-containing A-cluster of acetyl-CoA synthase (ACS) assembles acetyl-CoA from carbon monoxide (CO), a methyl group (CH(3)(+)), and coenzyme A (CoA). To accomplish this feat, ACS must bind CoA and interact with two other proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee7c92f39b921c5614068d47f021e31e
https://pubmed.ncbi.nlm.nih.gov/32937101
https://pubmed.ncbi.nlm.nih.gov/32937101
Autor:
Catherine L. Drennan, Elizabeth C. Wittenborn, Rachel A Hendrickson, Steven E. Cohen, Mehmet Can, Stephen W. Ragsdale
Publikováno v:
ACS
ACS Catalysis
ACS Catalysis
Copyright © 2020 American Chemical Society. The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-Co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bad420ef5ad7fde53ec5ef673f2ee99
https://hdl.handle.net/1721.1/133251
https://hdl.handle.net/1721.1/133251
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3d6abf17d9fb4e3bb4b4b1f400548cb
https://doi.org/10.7554/elife.39451
https://doi.org/10.7554/elife.39451