Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Danilo Ortillo"'
1
Spectroscopic Investigation of Pyruvate Formate Lyase-activating Enzyme: A Look into EPR, ENDOR and Mossabuer Spectroscopy
Autor: Danilo Ortillo, Joan B. Broderick
Publikováno v: Research Journal of Applied Sciences, Engineering and Technology. 8:1075-1097
Electron Paramagnetic Resonance (EPR) and Electron Nuclear Double Resonance (ENDOR) spectroscopies are extremely powerful and versatile methods for the characterization of paramagnetic systems in biology, chemistry and physics. For iron centers in th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0c599d4396bf5f95276957f8d55ae48d
https://doi.org/10.19026/rjaset.8.1072
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2
Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts
Autor: Clara Camaschella, Hong Ye, Manik C. Ghosh, Suh Young Jeong, Gennadiy Kovtunovych, Laura Silvestri, Naoya Uchida, John F. Tisdale, Tracey A. Rouault, Danilo Ortillo
Glutaredoxin 5 (GLRX5) deficiency has previously been identified as a cause of anemia in a zebrafish model and of sideroblastic anemia in a human patient. Here we report that GLRX5 is essential for iron-sulfur cluster biosynthesis and the maintenance
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f2451b710d25331a59c821709808180
https://europepmc.org/articles/PMC2860907/
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3
The iron-sulfur cluster of pyruvate formate-lyase activating enzyme in whole cells: cluster interconversion and a valence-localized [4Fe-4S]2+ state
Autor: Meng Li, Jian Yang, William E. Broderick, Danilo Ortillo, Sunil G. Naik, Joan B. Broderick, Boi Hanh Huynh, Ricardo Garcia-Serres
Publikováno v: Biochemistry. 48(39)
Pyruvate formate-lyase activating enzyme (PFL-AE) catalyzes the generation of a catalytically essential glycyl radical on pyruvate formate-lyase (PFL). Purified PFL-AE contains an oxygen-sensitive, labile [4Fe-4S] cluster that undergoes cluster inter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b23b40035bdef703ff11fc0055bcd47
https://pubmed.ncbi.nlm.nih.gov/19711960
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4
Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the 'radical-Sam' protein superfamily
Autor: William E. Broderick, Danilo Ortillo, Brian M. Hoffman, Joan B. Broderick, Mbako R. Nnyepi, Charles J. Walsby, Jian Yang
Publikováno v: Inorganic chemistry. 44(4)
Electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and Mössbauer spectroscopies and other physical methods have provided important new insights into the radical-SAM superfamily of proteins, which use iron-sulfur cluste
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::271a00e266497711513a813745c51f43
https://pubmed.ncbi.nlm.nih.gov/15859242
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6
An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme
Autor: Joan B. Broderick, Charles J. Walsby, William E. Broderick, Danilo Ortillo, Brian M. Hoffman
Publikováno v: Journal of the American Chemical Society. 124(38)
Pyruvate formate-lyase activating enzyme (PFL-AE) generates the catalytically essential glycyl radical on pyruvate formate-lyase via the interaction of the catalytically active [4Fe-4S]+ cluster with S-adenosylmethionine (AdoMet). Like other members
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17068c87dee217412fc3921cb3100ddb
https://pubmed.ncbi.nlm.nih.gov/12236732
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7
Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme
Autor: William E. Broderick, Brian M. Hoffman, Joan B. Broderick, Charles J. Walsby, Jennifer Cheek, Danilo Ortillo, Wei Hong
Publikováno v: Journal of the American Chemical Society. 124(12)
Pyruvate formate-lyase activating enzyme (PFL-AE) is a representative member of an emerging family of enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (AdoMet) to initiate radical catalysis. Although these enzymes have diverse funct
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aa36064a3f81adaedf2b7da8cfff938
https://pubmed.ncbi.nlm.nih.gov/11902903
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