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Journal articles
Redox Behavior of the S-Adenosylmethionine (SAM)-Binding Fe-S Cluster in Methylthiotransferase RimO, toward Understanding Dual SAM Activity
Thibaut Molle
1
Yohann Moreau
1
Martin Clémancey
1
Farhad Forouhar
2, 3
Jean-Luc Ravanat
4
Nicolas Duraffourg
1
Vincent Fourmond
5
Jean-Marc Latour
1
Serge Gambarelli
6
Etienne Mulliez
1, *
Mohamed Atta
1, *
*
Corresponding author
4
LAN - Laboratoire Lésions des Acides Nucléiques
SCIB - UMR E3 - Service de Chimie Inorganique et Biologique : DSM/INAC/SCIB
Jean-Luc Ravanat 4
Mail :
Author IdHAL : jean-luc-ravanat ORCID : https://orcid.org/0000-0002-7123-6358
Nicolas Duraffourg 1
Mail :
Author
Vincent Fourmond 5
Mail :
Author IdHAL : vincent-fourmond ORCID : https://orcid.org/0000-0001-9837-6214
Jean-Marc Latour 1
Mail :
Author
Serge Gambarelli 6
Mail :
Author
Etienne Mulliez 1
Mail :
Correspondent author
Mohamed Atta 1
Mail :
Correspondent author
1
LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux (17, rue des Martyrs 38054 Grenoble cedex 09 - France)
- IRIG - Institut de Recherche Interdisciplinaire de Grenoble : DRF/IRIG/DIESE (France)
- DRF (CEA) - Direction de Recherche Fondamentale (CEA) : DRF/IRIG (Direction de Recherche Fondamentale
Fundamental Research Division
CEA Saclay
91191 Gif-sur-Yvette
- France)
- CEA - Commissariat à l'énergie atomique et aux énergies alternatives (Centre de Saclay Centre de Grenoble Centre de Cadarache etc - France)
- DRF (CEA) - Direction de Recherche Fondamentale (CEA) : DRF/IRIG (Direction de Recherche Fondamentale
Fundamental Research Division
CEA Saclay
91191 Gif-sur-Yvette
- France)
- UGA [2016-2019] - Université Grenoble Alpes [2016-2019] (CS 40700 - 38058 Grenoble cedex - France)
- CNRS - Centre National de la Recherche Scientifique : UMR5249 (France)
2
Department of Biological Sciences, Columbia University, New York, New York, USA. (United States)
- Columbia University [New York] (Columbia University in the City of New York 2960 Broadway New York, NY 10027-6902 - United States)
3
Northeast Structural Genomics Consortium (United States)
- Columbia University [New York] (Columbia University in the City of New York 2960 Broadway New York, NY 10027-6902 - United States)
4
LAN - Laboratoire Lésions des Acides Nucléiques (17 rue des Martyrs 38054 Grenoble cedex 9 - France)
- SCIB - UMR E3 - Service de Chimie Inorganique et Biologique : DSM/INAC/SCIB (SCIB UMR E3, Institut Nanosciences et Cryogénie, CEA/Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9 - France)
- INAC - Institut Nanosciences et Cryogénie (CEA-Grenoble, 17 rue des Martyrs, F-38054 Grenoble cedex 9 - France)
- CEA - Commissariat à l'énergie atomique et aux énergies alternatives : DRF/INAC (Centre de Saclay Centre de Grenoble Centre de Cadarache etc - France)
- UGA [2016-2019] - Université Grenoble Alpes [2016-2019] : INAC (CS 40700 - 38058 Grenoble cedex - France)
- CNRS - Centre National de la Recherche Scientifique : FRE3200 (France)
- INAC - Institut Nanosciences et Cryogénie (CEA-Grenoble, 17 rue des Martyrs, F-38054 Grenoble cedex 9 - France)
5
BIP - Bioénergétique et Ingénierie des Protéines (CNRS - Université d’ Aix-Marseille
31, chemin Joseph Aiguier
13402 MARSEILLE Cedex 20 FRANCE
Tél : +33 (0)4 91 16 45 50 - France)
- AMU - Aix Marseille Université : UMR7281 (Aix-Marseille Université Jardins du Pharo 58 Boulevard Charles Livon 13284 Marseille cedex 7 - France)
- CNRS - Centre National de la Recherche Scientifique : UMR7281 (France)
6
SCIB - UMR E3 - Service de Chimie Inorganique et Biologique (SCIB UMR E3, Institut Nanosciences et Cryogénie, CEA/Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9 - France)
- INAC - Institut Nanosciences et Cryogénie (CEA-Grenoble, 17 rue des Martyrs, F-38054 Grenoble cedex 9 - France)
- CEA - Commissariat à l'énergie atomique et aux énergies alternatives : DRF/INAC (Centre de Saclay Centre de Grenoble Centre de Cadarache etc - France)
- UGA [2016-2019] - Université Grenoble Alpes [2016-2019] : INAC (CS 40700 - 38058 Grenoble cedex - France)
- CNRS - Centre National de la Recherche Scientifique : FRE3200 (France)
Abstract : RimO, a radical-S-adenosylmethionine (SAM) enzyme, catalyzes the specific C3 methylthiolation of the D89 residue in the ribosomal S12 protein. Two intact iron–sulfur clusters and two SAM cofactors both are required for catalysis. By using electron paramagnetic resonance, Mössbauer spectroscopies, and site-directed mutagenesis, we show how two SAM molecules sequentially bind to the unique iron site of the radical-SAM cluster for two distinct chemical reactions in RimO. Our data establish that the two SAM molecules bind the radical-SAM cluster to the unique iron site, and spectroscopic evidence obtained under strongly reducing conditions supports a mechanism in which the first molecule of SAM causes the reoxidation of the reduced radical-SAM cluster, impeding reductive cleavage of SAM to occur and allowing SAM to methylate a HS– ligand bound to the additional cluster. Furthermore, by using density functional theory-based methods, we provide a description of the reaction mechanism that predicts the attack of the carbon radical substrate on the methylthio group attached to the additional [4Fe-4S] cluster.
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Journal articles
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https://hal-amu.archives-ouvertes.fr/hal-01414834
Contributor : Laure Azzopardi <>
Submitted on : Monday, December 12, 2016 - 3:59:14 PM
Last modification on : Thursday, July 9, 2020 - 9:43:19 AM
Contributor : Laure Azzopardi <>
Submitted on : Monday, December 12, 2016 - 3:59:14 PM
Last modification on : Thursday, July 9, 2020 - 9:43:19 AM
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- HAL Id : hal-01414834, version 1
- DOI : 10.1021/acs.biochem.6b00597
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Citation
Thibaut Molle, Yohann Moreau, Martin Clémancey, Farhad Forouhar, Jean-Luc Ravanat, et al.. Redox Behavior of the S-Adenosylmethionine (SAM)-Binding Fe-S Cluster in Methylthiotransferase RimO, toward Understanding Dual SAM Activity. Biochemistry, American Chemical Society, 2016, 55 (41), pp.5798-5808. ⟨10.1021/acs.biochem.6b00597⟩. ⟨hal-01414834⟩
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