Výsledky vyhledávání - "Douglas M, Warui"

Functional spectrum and specificity of mitochondrial ferredoxins FDX1 and FDX2

Autor: Vinzent Schulz, Somsuvro Basu, Sven-A. Freibert, Holger Webert, Linda Boss, Ulrich Mühlenhoff, Fabien Pierrel, Lars-O. Essen, Douglas M. Warui, Squire J. Booker, Oliver Stehling, Roland Lill

Publikováno v: Nature Chemical Biology. 19:206-217

Ferredoxins comprise a large family of iron-sulfur (Fe-S) proteins that shuttle electrons in diverse biological processes. Human mitochondria contain two isoforms of [2Fe-2S] ferredoxins, FDX1 (aka adrenodoxin) and FDX2, with known functions in cytoc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1845ac316956605a467f82d2aea00d31
https://doi.org/10.1038/s41589-022-01159-4

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FDX1 regulates cellular protein lipoylation through direct binding to LIAS

Autor: Margaret B. Dreishpoon, Nolan R. Bick, Boryana Petrova, Douglas M. Warui, Alison Cameron, Squire J. Booker, Naama Kanarek, Todd R. Golub, Peter Tsvetkov

Publikováno v: bioRxiv

Ferredoxins are a family of iron-sulfur (Fe-S) cluster proteins that serve as essential electron donors in numerous cellular processes that are conserved through evolution. The promiscuous nature of ferredoxins as electron donors enables them to part

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b384419c717b788121c1dff5b1da05b2
https://europepmc.org/articles/PMC9915701/

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In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1

Autor: Douglas M. Warui, Debangsu Sil, Kyung-Hoon Lee, Syam Sundar Neti, Olga A. Esakova, Hayley L. Knox, Carsten Krebs, Squire J. Booker

Publikováno v: ACS biomed chem Au. 2(5)

Lipoyl synthase (LS) catalyzes the last step in the biosynthesis of the lipoyl cofactor, which is the attachment of sulfur atoms at C6 and C8 of an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d66aa4221a8eee66c6588872b9862db
https://pubmed.ncbi.nlm.nih.gov/36281303

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[FeFe]‐Hydrogenase: Defined Lysate‐Free Maturation Reveals a Key Role for Lipoyl‐H‐Protein in DTMA Ligand Biosynthesis

Autor: Adrien Pagnier, Batuhan Balci, Eric M. Shepard, Hao Yang, Douglas M. Warui, Stella Impano, Squire J. Booker, Brian M. Hoffman, William E. Broderick, Joan B. Broderick

Publikováno v: Angew Chem Int Ed Engl

Maturation of [FeFe]-hydrogenase (HydA) involves synthesis of a CO, CN(−), and dithiomethylamine (DTMA)-coordinated 2Fe subcluster that is inserted into HydA to make the active hydrogenase. This process requires three maturation enzymes: the radica

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a09661f5a4c7ab764336759118505ab9
https://doi.org/10.1002/anie.202203413

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Characterization of LipS1 and LipS2 from

Autor: Syam Sundar, Neti, Debangsu, Sil, Douglas M, Warui, Olga A, Esakova, Amy E, Solinski, Dante A, Serrano, Carsten, Krebs, Squire J, Booker

Publikováno v: ACS biomed chem Au. 2(5)

Lipoic acid is an eight-carbon sulfur-containing biomolecule that functions primarily as a cofactor in several multienzyme complexes. It is biosynthesized as an attachment to a specific lysyl residue on one of the subunits of these multienzyme comple

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::99ea8f1085a62d0823fa750ef8aa46cc
https://pubmed.ncbi.nlm.nih.gov/36281299

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An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase

Autor: Neela H. Yennawar, Alexey Silakov, Squire J. Booker, Douglas M. Warui, Tyler L. Grove, Olga Esakova

Publikováno v: Journal of the American Chemical Society. 141:14142-14151

Quinolinic acid (QA) is a common intermediate in the biosynthesis of nicotinamide adenine dinucleotide (NAD(+)) and its derivatives in all organisms that synthesize the molecule de novo. In most prokaryotes, it is formed from the condensation of dihy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::122ba9159dab39905c57fa05e59fa5c5
https://doi.org/10.1021/jacs.9b02513

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Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism

Autor: Lauren J. Rajakovich, Carsten Krebs, Ning Li, J. Martin Bollinger, Hanne Nørgaard, Squire J. Booker, Douglas M. Warui, Wei-Chen Chang, Maria-Eirini Pandelia

Publikováno v: Journal of the American Chemical Society. 137(36)

Aldehyde-deformylating oxygenase (ADO) is a ferritin-like nonheme-diiron enzyme that catalyzes the last step in a pathway through which fatty acids are converted into hydrocarbons in cyanobacteria. ADO catalyzes conversion of a fatty aldehyde to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21d9f7ef34c66b8cff088d98ac7c59b5
https://pubmed.ncbi.nlm.nih.gov/26284355

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