Zobrazeno 1 - 10
of 127
pro vyhledávání: '"Catherine L. Drennan"'
Publikováno v:
ACS Omega
ACS Omega, Vol 6, Iss 21, Pp 13756-13765 (2021)
ACS Omega, Vol 6, Iss 21, Pp 13756-13765 (2021)
Tuberculosis (TB) is the deadliest infectious disease in the world. In Mycobacterium tuberculosis, the first committed step in sulfate assimilation is the reductive cleavage of adenosine-5'-phosphosulfate (APS) to form adenosine-5'-phosphate (AMP) an
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
Publikováno v:
Science
Caught in the act Proton-coupled electron transfer (PCET) is an important process for moving electrons through proteins and requires precise positioning of suitable proton and electron carriers. Kang et al. determined a cryo–electron microscopy str
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:
Stacey D. Wetmore, Ke Bian, Marco Jost, Catherine L. Drennan, Fangyi Chen, Deyu Li, Stefan A. P. Lenz, Rui Qi, Qi Tang, John M. Essigmann
Publikováno v:
Nucleic Acids Research
5-Methylcytosine (5mC) in DNA CpG islands is an important epigenetic biomarker for mammalian gene regulation. It is oxidized to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5-carboxylcytosine (5caC) by the ten-eleven translocation (TET
Autor:
William M. Kincannon, Nathan A. Bruender, Elizabeth J. Blaesi, Vahe Bandarian, Catherine L. Drennan, Tsehai A.J. Grell, Carsten Krebs
Publikováno v:
The Journal of Biological Chemistry
Sactipeptides are a subclass of ribosomally synthesized and post-translationally modified peptides (RiPPs). They contain a unique thioether bond, referred to as a sactionine linkage, between the sulfur atom of a cysteine residue and the α-carbon of
Autor:
Maanasa Narayanamoorthy, Chaoxiang Ren, Antonio Del Rio Flores, Jan Paulo T. Zaragoza, Wenjun Zhang, Heather J. Kulik, Wenlong Cai, Rimsha Mehmood, Rohan Jonnalagadda, Catherine L. Drennan
Publikováno v:
The Journal of Biological Chemistry
Elsevier
Elsevier
The isonitrile moiety is found in marine sponges and some microbes, where it plays a role in processes such as virulence and metal acquisition. Until recently only one route was known for isonitrile biosynthesis, a condensation reaction that brings t
Publikováno v:
The Journal of Biological Chemistry
Pyruvate formate-lyase (PFL) is a glycyl radical enzyme (GRE) that converts pyruvate and coenzyme A into acetyl-CoA and formate in a reaction that is crucial to the primary metabolism of many anaerobic bacteria. The glycyl radical cofactor, which is
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