Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Caroline Marchi-Delapierre"'
Autor:
Céline Reynaud, Hassan Hazimeh, Jean-Marc Mattalia, Caroline Marchi-Delapierre, Michel Chanon
Publikováno v:
ARKIVOC, Vol 2011, Iss 10, Pp 33-43 (2011)
Externí odkaz:
https://doaj.org/article/a3a702dabe0a4920bc37ae7808df8684
Publikováno v:
ARKIVOC, Vol 2006, Iss 4, Pp 90-118 (2006)
Externí odkaz:
https://doaj.org/article/d26bab3eecd64d1da35d68c024337e55
Publikováno v:
Chemistry-A European Journal
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, 26 (70), pp.16633-16638. ⟨10.1002/chem.202003746⟩
Chemistry-A European Journal, 2020, 26 (70), pp.16633-16638. ⟨10.1002/chem.202003746⟩
Chemistry-A European Journal, Wiley-VCH Verlag, 2020, 26 (70), pp.16633-16638. ⟨10.1002/chem.202003746⟩
Chemistry-A European Journal, 2020, 26 (70), pp.16633-16638. ⟨10.1002/chem.202003746⟩
International audience; Performing a heterogeneous catalysis with proteins is still a challenge. Herein, we demonstrate the importance of cross‐linked crystals for sulfoxide oxidation by an artificial enzyme. The biohybrid consists of the insertion
Autor:
David Michael Mayes, Sarah Lopez, Chloé Leprêtre, Yohann Moreau, Christine Cavazza, Stéphane Ménage, Caroline Marchi-Delapierre, Serge Crouzy, Nicolai Burzlaff
Publikováno v:
ACS Catalysis
ACS Catalysis, American Chemical Society, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, American Chemical Society, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
ACS Catalysis, 2020, 10 (10), pp.5631-5645. ⟨10.1021/acscatal.9b04904⟩
International audience; Artificial enzymes represent an attractive alternative to design abiotic biocatalysis. EcNikA-Rul, an artificial metalloenzyme developed by embedding a ruthenium-based catalyst into the cavity of the periplasmic nickel-binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1e7f4c47df4ae2f4817a1092dda188a
https://hal.archives-ouvertes.fr/hal-02865406
https://hal.archives-ouvertes.fr/hal-02865406
Publikováno v:
Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications
Diéguez Montserrat-Bäckvall Jan-E⋅and Pàmies Oscar. Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications, Chap. 7, Wiley-VCH Verlag GmbH & Co. KGaA, pp.199-224, 2018, ⟨10.1002/9783527804085.ch7⟩
Artificial Metalloenzymes and MetalloDNAzymes in Catalysis ISBN: 9783527804085
Artificial Metalloenzymes and MetalloDNAzymes in Catalysis
Diéguez Montserrat-Bäckvall Jan-E⋅and Pàmies Oscar. Artificial Metalloenzymes and MetalloDNAzymes in Catalysis: From Design to Applications, Chap. 7, Wiley-VCH Verlag GmbH & Co. KGaA, pp.199-224, 2018, ⟨10.1002/9783527804085.ch7⟩
Artificial Metalloenzymes and MetalloDNAzymes in Catalysis ISBN: 9783527804085
Artificial Metalloenzymes and MetalloDNAzymes in Catalysis
International audience; Artificial metalloenzymes broadens the scope of possibilities for catalysis at the crossroad of biocatalysis and metal‐based catalysis. The content of this chapter illustrates this outline in the field of oxidation, thanks t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4a5e1c2b53f3598bd12ae19a4cbd999
https://hal.archives-ouvertes.fr/hal-02019550
https://hal.archives-ouvertes.fr/hal-02019550
Autor:
Marina Iannello, Sarah Lopez, Caroline Marchi-Delapierre, Stéphane Ménage, Frank Strinitz, Nicolai Burzlaff, Laurianne Rondot, Christine Cavazza, Adeline Jorge-Robin, Elisabetta Boeri-Erba
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2017, 53 (25), pp.3579-3582. ⟨10.1039/C6CC08873B⟩
Chemical Communications, 2017, 53 (25), pp.3579-3582. ⟨10.1039/C6CC08873B⟩
Chemical Communications, Royal Society of Chemistry, 2017, 53 (25), pp.3579-3582. ⟨10.1039/C6CC08873B⟩
Chemical Communications, 2017, 53 (25), pp.3579-3582. ⟨10.1039/C6CC08873B⟩
International audience; Artificial enzymes are required to catalyse non-natural reactions. Here, a hybrid catalyst was developed by embedding a novel Ru complex in the transport protein NikA. The protein scaffold activates the bound Ru complex to pro
Publikováno v:
Israel Journal of Chemistry
Israel Journal of Chemistry, 2015, 55 (1 SI), pp.61-75. ⟨10.1002/ijch.201400110⟩
Israel Journal of Chemistry, Wiley-VCH Verlag, 2015, 55 (1 SI), pp.61-75. ⟨10.1002/ijch.201400110⟩
Israel Journal of Chemistry, 2015, 55 (1 SI), pp.61-75. ⟨10.1002/ijch.201400110⟩
Israel Journal of Chemistry, Wiley-VCH Verlag, 2015, 55 (1 SI), pp.61-75. ⟨10.1002/ijch.201400110⟩
International audience; The principle of enzyme mimics has been raised to its pinnacle by the design of hybrids made from inorganic complexes embedded into biomolecules. The present review focuses on the design of artificial metalloenzymes for oxidat
Autor:
Patricia Amara, Frédéric Oddon, Caroline Marchi-Delapierre, Charlène Esmieu, Adeline Jorge-Robin, Stéphane Ménage, Mickaël V. Cherrier, Marina Iannello, Elodie Girgenti, Christine Cavazza
Publikováno v:
Angewandte Chemie. 125:4014-4017
Autor:
Adeline Jorge-Robin, Frédéric Oddon, Laurianne Rondot, Elodie Girgenti, Stéphane Ménage, Caroline Marchi-Delapierre
Publikováno v:
Journal of Molecular Catalysis A: Chemical
Journal of Molecular Catalysis A: Chemical, 2016, 416, pp.20-28. ⟨10.1016/j.molcata.2016.02.015⟩
Journal of Molecular Catalysis A: Chemical, Elsevier, 2016, 416, pp.20-28. ⟨10.1016/j.molcata.2016.02.015⟩
Journal of Molecular Catalysis A: Chemical, 2016, 416, pp.20-28. ⟨10.1016/j.molcata.2016.02.015⟩
Journal of Molecular Catalysis A: Chemical, Elsevier, 2016, 416, pp.20-28. ⟨10.1016/j.molcata.2016.02.015⟩
International audience; A new artificial oxidase has been developed for selective transformation of thioanisole. The catalytic activity of an iron inorganic complex, FeLibu, embedded in a transport protein NikA has been investigated in aqueous media.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08209c5c1ff54074eed05cdb2caeb772
https://hal.science/hal-01323912
https://hal.science/hal-01323912
Autor:
Frédéric Oddon, Elodie Girgenti, Stéphane Ménage, Jacques Pécaut, Colette Lebrun, Caroline Marchi-Delapierre
Publikováno v:
European Journal of Inorganic Chemistry. 2012:85-96
A biomimetic approach based on Rieske dioxygenase mimics has been undertaken, which uses the tetradentate N2Py2 ligand platform that contains two pyridine moieties linked to a 1,2-diaminoethane or a trans-1,2-diaminocyclohexane backbone. Here we repo