Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe–S Cluster Biosynthesis

Autor: Batoul Srour, Sylvain Gervason, Maren Hellen Hoock, Beata Monfort, Kristian Want, Djabir Larkem, Nadine Trabelsi, Gautier Landrot, Andrea Zitolo, Emiliano Fonda, Emilien Etienne, Guillaume Gerbaud, Christina Sophia Müller, Jonathan Oltmanns, Jesse B. Gordon, Vishal Yadav, Malgorzata Kleczewska, Marcin Jelen, Michel B. Toledano, Rafal Dutkiewicz, David P. Goldberg, Volker Schünemann, Bruno Guigliarelli, Bénédicte Burlat, Christina Sizun, Benoit D’Autréaux

Publikováno v: Journal of the American Chemical Society
Journal of the American Chemical Society, 2022, 144 (38), pp.17496-17515. ⟨10.1021/jacs.2c06338⟩

International audience; Iron−sulfur (Fe−S) clusters are prosthetic groups of proteins biosynthesized on scaffold proteins by highly conserved multi-protein machineries. Biosynthesis of Fe−S clusters into the ISCU scaffold protein is initiated b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f1e62412505c0e54f958b4c5b661c5
https://doi.org/10.1021/jacs.2c06338

A Reactive, Photogenerated High-Spin (

Autor: Jesse B, Gordon, Therese, Albert, Aniruddha, Dey, Sinan, Sabuncu, Maxime A, Siegler, Eckhard, Bill, Pierre, Moënne-Loccoz, David P, Goldberg

Publikováno v: J Am Chem Soc

Addition of dioxygen at low temperature to the nonheme ferrous complex, Fe(II)(Me(3)TACN)(OSi(Ph2))(2)O) (1), in 2-MeTHF produces a peroxo-bridged diferric complex, Fe(2)(III)(μ-O(2))(Me(3)TACN)(2)((OSi(Ph2))(2)O)(2) (2), which was characterized by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3b3c5737dc8caf8be07f4facfdf08907
https://pubmed.ncbi.nlm.nih.gov/34913683

Concerted Differential Changes of Helical Dynamics and Packing upon Ligand Occupancy in a Bacterial Chemoreceptor

Autor: Gabriela S. Schlau-Cohen, Mikaila C Hoffman, Julianne M Troiano, Jesse B. Gordon, Mingshan Li, Gerald L. Hazelbauer

Publikováno v: ACS Chem Biol

Transmembrane receptors are central components of the chemosensory systems by which motile bacteria detect and respond to chemical gradients. An attractant bound to the receptor periplasmic domain generates conformational signals that regulate a hist

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8521971a070cdc00aac009e83a45c5e
https://doi.org/10.1021/acschembio.1c00576

Proton-Coupled Electron-Transfer Reactivity Controls Iron versus Sulfur Oxidation in Nonheme Iron–Thiolate Complexes

Autor: Jesse B. Gordon, David P. Goldberg, Maxime A. Siegler, Jeremy P. McGale

Publikováno v: Inorg Chem

Reaction of the 5-coordinate Fe(II)(N(4)S) complexes, [Fe(II)(iPr(3)TACN)(abt(x))](OTf) (abt = aminobenzenethiolate, X = H, CF(3)) with a one-electron oxidant and an appropriate base leads to net H-atom loss, generating new Fe(III)(iminobenzenethiola

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9a70d09d3b2e866abef206419cb22f2
https://doi.org/10.1021/acs.inorgchem.0c03779

Activation of Dioxygen by a Mononuclear Nonheme Iron Complex: Sequential Peroxo, Oxo, and Hydroxo Intermediates

Autor: Kyle M. Lancaster, Samantha N. MacMillan, David P. Goldberg, Pierre Moënne-Loccoz, Avery C. Vilbert, Ida M. DiMucci, Jesse B. Gordon

Publikováno v: J Am Chem Soc

The activation of dioxygen by Fe(II)(Me(3)TACN)(S(2)SiMe(2)) (1) is reported. Reaction of 1 with O(2) at −135 °C in 2-MeTHF generates a thiolate-ligated (peroxo)diiron complex Fe(III)(2)(O(2))(Me(3)TACN)(2)(S(2)SiMe(2))(2) (2) that was characteriz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9389a7ca50dabd6e9aaa4cf78948f375
https://doi.org/10.1021/jacs.9b05274