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pro vyhledávání: '"Steven E. Cohen"'
Autor:
Steven E. Cohen, Catherine L. Drennan, Andrew C. Weitz, Michael P. Hendrich, Sean Elliott, Kimberly Rizzolo
Publikováno v:
J Am Chem Soc
BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)=O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here
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
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
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:
Steven E. Cohen, Catherine L. Drennan, Madeline M. López Muñoz, Andrew C. Weitz, Sean Elliott, Michael P. Hendrich, Kimberly Rizzolo
Publikováno v:
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H2O2) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we