Simon Arragain

ORCID: 0000-0002-6500-0066
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • RNA modifications and cancer
  • Electrocatalysts for Energy Conversion
  • Porphyrin Metabolism and Disorders
  • Metal-Organic Frameworks: Synthesis and Applications
  • Metal-Catalyzed Oxygenation Mechanisms
  • Photosynthetic Processes and Mechanisms
  • Polyoxometalates: Synthesis and Applications
  • RNA and protein synthesis mechanisms
  • Ammonia Synthesis and Nitrogen Reduction
  • Inorganic Chemistry and Materials
  • Biofuel production and bioconversion
  • Folate and B Vitamins Research
  • Ferrocene Chemistry and Applications
  • Peroxisome Proliferator-Activated Receptors
  • Algal biology and biofuel production
  • Carbon dioxide utilization in catalysis
  • Nanocluster Synthesis and Applications
  • Cancer-related gene regulation
  • Microbial Metabolic Engineering and Bioproduction
  • Biochemical and Molecular Research
  • Chemical Analysis and Environmental Impact
  • Lipid metabolism and biosynthesis
  • Redox biology and oxidative stress
  • Hydrogen Storage and Materials

IFP Énergies nouvelles
2021-2024

Sorbonne Université
2017-2022

Centre National de la Recherche Scientifique
2009-2022

Laboratoire de chimie des processus biologiques
2017-2022

Collège de France
2017-2022

University of California, Davis
2021

Concordia University
2018

Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria
2017

Centre for Plant Biotechnology and Genomics
2014-2017

Universidad Politécnica de Madrid
2014-2017

Bacterial and eukaryotic transfer RNAs have been shown to contain hypermodified adenosine, 2-methylthio-N(6)-threonylcarbamoyladenosine, at position 37 (A(37)) adjacent the 3'-end of anticodon, which is essential for efficient highly accurate protein translation by ribosome. Using a combination bioinformatic sequence analysis in vivo assay coupled HPLC/MS technique, we identified, from distinct signatures, two methylthiotransferase (MTTase) subfamilies, designated as MtaB bacterial cells...

10.1074/jbc.m110.106831 article EN cc-by Journal of Biological Chemistry 2010-06-29

Organelles are intracellular compartments which themselves compartmentalized. Biogenic and metabolic processes localized to specialized domains or microcompartments enhance their efficiency suppress deleterious side reactions. An example of intra-organellar compartmentalization is the pyrenoid in chloroplasts algae hornworts. This microcompartment enhances photosynthetic CO2-fixing activity Calvin-Benson cycle enzyme Rubisco, suppresses an energetically wasteful oxygenase mitigates limiting...

10.1371/journal.pone.0185039 article EN cc-by PLoS ONE 2018-02-26

Significance Posttranscriptional modifications of tRNA are essential for translational fidelity. More specifically, mechanisms selective sulfuration tRNAs still largely unknown, and the enzymes responsible these reactions incompletely investigated. Therefore, characterizing such systems at molecular level is greatly valuable to our understanding a whole class modification reactions. We study TtuA, representative member enzyme superfamily, show that it intriguingly catalyzes nonredox sulfur...

10.1073/pnas.1700902114 article EN Proceedings of the National Academy of Sciences 2017-06-27

Abstract Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of class ferredoxins harboring [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) is detected in germinating seeds. recombinant purified produced from Escherichia coli , although very unstable, exhibits DGAT activity vitro . A shorter version devoid its N-terminal...

10.1038/s41598-018-35545-7 article EN cc-by Scientific Reports 2018-11-16

Post-translational modifications of ribosomal proteins are important for the accuracy decoding machinery. A recent in vivo study has shown that rimO gene is involved generation 3-methylthio derivative residue Asp-89 protein S12 (Anton, B. P., Saleh, L., Benner, J. S., Raleigh, E. A., Kasif, and Roberts, R. (2008) Proc. Natl. Acad. Sci. U. S. A. 105, 1826-1831). This reaction formally identical to catalyzed by MiaB on C2 adenosine 37 near anticodon several tRNAs. We present spectroscopic...

10.1074/jbc.m109.065516 article EN cc-by Journal of Biological Chemistry 2009-12-10

NifB utilizes two equivalents of S-adenosyl methionine (SAM) to insert a carbide atom and fuse substrate [Fe-S] clusters forming the cofactor (NifB-co), which is then passed NifEN for further modification form iron-molybdenum (FeMo-co) nitrogenase. Here, we demonstrate that from methanogen Methanocaldococcus infernus radical SAM enzyme able reductively cleave 5'-deoxyadenosine competent in FeMo-co maturation. Using electron paramagnetic resonance spectroscopy have characterized three...

10.1021/jacs.6b03329 article EN Journal of the American Chemical Society 2016-06-06

One of the main hurdles to engineer nitrogenase in a non-diazotrophic host is achieving NifB activity. an extremely unstable and oxygen sensitive protein that catalyzes low-potential SAM-radical dependent reaction. The product activity called NifB-co, complex [8Fe-9S-C] cluster serves as obligate intermediate biosyntheses active-site cofactors all known nitrogenases. Here we study diversity phylogeny naturally occurring proteins, their architecture functions distinct domains order understand...

10.3389/fpls.2017.01947 article EN cc-by Frontiers in Plant Science 2017-11-14

Plant biomass can be converted to bioproducts using fungal enzymatic cocktails that have been improved by the implementation of lytic polysaccharide monooxygenases (LPMOs) known boost cellulases. However, due complexity their oxidative catalysis, it is still difficult properly control and sustain LPMO activity. Here, we investigated whether natural partner LPMOs, i.e., cellobiose dehydrogenase (CDH), could a promising solution. To this end, reconstituted minimal cocktail main cellulases from...

10.1021/acssuschemeng.4c00851 article EN ACS Sustainable Chemistry & Engineering 2024-05-16

Abstract Lytic polysaccharide monooxygenases (LPMOs) are taxonomically widespread copper-enzymes boosting biopolymers conversion (e.g. cellulose, chitin) in Nature. White-rot Polyporales, which major fungal wood decayers, may possess up to 60 LPMO-encoding genes belonging the auxiliary activities family 9 (AA9). Yet, functional relevance of such multiplicity remains be uncovered. Previous comparative transcriptomic studies six Polyporales fungi grown on cellulosic substrates had shown...

10.1038/s41598-023-38617-5 article EN cc-by Scientific Reports 2023-07-18

[FeFe] hydrogenases are enzymes that have acquired a unique capacity to synthesize or consume molecular hydrogen (H

10.1016/j.bpj.2023.03.027 article EN cc-by-nc-nd Biophysical Journal 2023-03-23

[FeFe] hydrogenases are highly active catalysts for the interconversion of molecular hydrogen with protons and electrons. Here, we use a combination isotopic labeling, 57Fe nuclear resonance vibrational spectroscopy (NRVS), density functional theory (DFT) calculations to observe characterize modes involving motion 2-azapropane-1,3-dithiolate (ADT) ligand bridging two iron sites in [2Fe]H subcluster. A −13C2H2– ADT labeling synthetic diiron precursor produced isotope effects observed...

10.1021/jacs.1c02323 article EN Journal of the American Chemical Society 2021-05-27
Coming Soon ...