Zobrazeno 1 - 10
of 23
pro vyhledávání: '"heme protein models"'
Autor:
Linda Leone, Daniele D'Alonzo, Véronique Balland, Gerardo Zambrano, Marco Chino, Flavia Nastri, Ornella Maglio, Vincenzo Pavone, Angela Lombardi
Publikováno v:
Frontiers in Chemistry, Vol 6 (2018)
Manganese-porphyrins are important tools in catalysis, due to their capability to promote a wide variety of synthetically valuable transformations. Despite their great reactivity, the difficulties to control the reaction selectivity and to protect th
Externí odkaz:
https://doaj.org/article/0fedd8ff08a14c7caecc7f3b717aa4af
Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts
Autor:
Claudia Vicari, Angela Lombardi, Ricardo O. Louro, Ornella Maglio, Marco Chino, Vincenzo Pavone
Publikováno v:
Chemical communications (Lond., 1996, Online) 57 (2021): 990–993. doi:10.1039/d0cc06676a
info:cnr-pdr/source/autori:Maglio, Ornella; Chino, Marco; Vicari, Claudia; Pavone, Vincenzo; Louro, Ricardo O; Lombardi, Angela/titolo:Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts/doi:10.1039%2Fd0cc06676a/rivista:Chemical communications (Lond., 1996, Online)/anno:2021/pagina_da:990/pagina_a:993/intervallo_pagine:990–993/volume:57
Chemical Communications
info:cnr-pdr/source/autori:Maglio, Ornella; Chino, Marco; Vicari, Claudia; Pavone, Vincenzo; Louro, Ricardo O; Lombardi, Angela/titolo:Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts/doi:10.1039%2Fd0cc06676a/rivista:Chemical communications (Lond., 1996, Online)/anno:2021/pagina_da:990/pagina_a:993/intervallo_pagine:990–993/volume:57
Chemical Communications
Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aac2914f7d87a7ec1f00c869176dc07e
http://www.cnr.it/prodotto/i/443558
http://www.cnr.it/prodotto/i/443558
Publikováno v:
Biotechnology and applied biochemistry 67 (2020): 495–515. doi:10.1002/bab.1985
info:cnr-pdr/source/autori:Leone, Linda; Chino, Marco; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Mimochrome, a metalloporphyrin-based catalytic Swiss knife+/doi:10.1002%2Fbab.1985/rivista:Biotechnology and applied biochemistry/anno:2020/pagina_da:495/pagina_a:515/intervallo_pagine:495–515/volume:67
info:cnr-pdr/source/autori:Leone, Linda; Chino, Marco; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Mimochrome, a metalloporphyrin-based catalytic Swiss knife+/doi:10.1002%2Fbab.1985/rivista:Biotechnology and applied biochemistry/anno:2020/pagina_da:495/pagina_a:515/intervallo_pagine:495–515/volume:67
Over the years, mimochromes, a class of miniaturized porphyrin-based metalloproteins, have proven to be reliable but still versatile scaffolds. After two decades from their birth, we retrospectively review our work in mimochrome design and engineerin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e992c10d838b9a950c02d322233c581
Autor:
Gerardo Zambrano, Ornella Maglio, Marco Chino, Vincenzo Pavone, Linda Leone, Daniele D'Alonzo, Véronique Balland, Flavia Nastri, Angela Lombardi
Publikováno v:
Frontiers in Chemistry
Frontiers in Chemistry, Vol 6 (2018)
Frontiers in Chemistry 6 (2018). doi:10.3389/fchem.2018.00590
info:cnr-pdr/source/autori:Leone, Linda; D'Alonzo, Daniele; Balland, Véronique; Zambrano, Gerardo; Chino, Marco; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Mn-Mimochrome VI*a: An artificial metalloenzyme with peroxygenase activity/doi:10.3389%2Ffchem.2018.00590/rivista:Frontiers in Chemistry/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:6
Frontiers in Chemistry, Vol 6 (2018)
Frontiers in Chemistry 6 (2018). doi:10.3389/fchem.2018.00590
info:cnr-pdr/source/autori:Leone, Linda; D'Alonzo, Daniele; Balland, Véronique; Zambrano, Gerardo; Chino, Marco; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Mn-Mimochrome VI*a: An artificial metalloenzyme with peroxygenase activity/doi:10.3389%2Ffchem.2018.00590/rivista:Frontiers in Chemistry/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:6
Manganese-porphyrins are important tools in catalysis, due to their capability to promote a wide variety of synthetically valuable transformations. Despite their great reactivity, the difficulties to control the reaction selectivity and to protect th
Autor:
Daniele D'Alonzo, Marco Chino, Gerardo Zambrano, Ornella Maglio, Giorgio Caserta, Flavia Nastri, Vincenzo Pavone, Vincenzo Firpo, Linda Leone, Angela Lombardi
Publikováno v:
ChemBioChem
19 (2018): 1823–1826. doi:10.1002/cbic.201800200
info:cnr-pdr/source/autori:Caserta, Giorgio; Chino, Marco; Firpo, Vincenzo; Zambrano, Gerardo; Leone, Linda; D'Alonzo, Daniele; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design/doi:10.1002%2Fcbic.201800200/rivista:ChemBioChem (Print)/anno:2018/pagina_da:1823/pagina_a:1826/intervallo_pagine:1823–1826/volume:19
19 (2018): 1823–1826. doi:10.1002/cbic.201800200
info:cnr-pdr/source/autori:Caserta, Giorgio; Chino, Marco; Firpo, Vincenzo; Zambrano, Gerardo; Leone, Linda; D'Alonzo, Daniele; Nastri, Flavia; Maglio, Ornella; Pavone, Vincenzo; Lombardi, Angela/titolo:Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design/doi:10.1002%2Fcbic.201800200/rivista:ChemBioChem (Print)/anno:2018/pagina_da:1823/pagina_a:1826/intervallo_pagine:1823–1826/volume:19
Rational design provides an attractive strategy to tune and control the reactivity of bioinspired catalysts. While there has been considerable progress in the design of heme oxidase mimetics with active site environments of ever-growing complexity an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97fa841d570b23d811a1e2632d7f1ade
https://publications.cnr.it/doc/443541
https://publications.cnr.it/doc/443541
Autor:
Vorburger, Pauline, Lo, Mamadou, Choua, Sylvie, Bernard, Maxime, Melin, Frederic, Oueslati, N, Boudon, Corinne, Elhabiri, Mourad, Wytko-weiss, Jennifer, Hellwig, Petra, Weiss, Jean
Publikováno v:
Inorganica Chimica Acta
Inorganica Chimica Acta, Elsevier, 2017, 468, pp.232-238. ⟨10.1016/j.ica.2017.04.052⟩
Inorganica Chimica Acta, Elsevier, 2017, 468, pp.232-238. ⟨10.1016/j.ica.2017.04.052⟩
The structure-property relationships were compared for the iron and iron-copper complexes of two functional cytochrome c oxidase models, 1 and 2, both constructed upon a phenanthroline-strapped porphyrin bearing respectively pyridyl or picolinyl buil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::b905fc0aeefcbf3aca0426a9bd4b0fc1
https://hal.archives-ouvertes.fr/hal-02177402
https://hal.archives-ouvertes.fr/hal-02177402
Autor:
Linda Leone, Diaa Aref, Vincenzo Firpo, Angela Lombardi, Flavia Nastri, Marco Chino, Gerardo Zambrano, Ornella Maglio, Luca Lista, Daniele D'Alonzo, Fabio Pirro
Publikováno v:
Biopolymers
info:cnr-pdr/source/autori:Chino, Marco; Leone, Linda; Zambrano, Gerardo; Pirro, Fabio; D'Alonzo, Daniele; Firpo, Vincenzo; Aref, Diaa; Lista, Liliana; Maglio, Ornella; Nastri, Flavia; Lombardi, Angela/titolo:Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages/doi:10.1002%2Fbip.23107/rivista:Biopolymers (Print)/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:109
info:cnr-pdr/source/autori:Chino, Marco; Leone, Linda; Zambrano, Gerardo; Pirro, Fabio; D'Alonzo, Daniele; Firpo, Vincenzo; Aref, Diaa; Lista, Liliana; Maglio, Ornella; Nastri, Flavia; Lombardi, Angela/titolo:Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages/doi:10.1002%2Fbip.23107/rivista:Biopolymers (Print)/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:109
Inspired by natural heme-proteins, scientists have attempted for decades to design efficient and selective metalloporphyrin-based oxidation catalysts. Starting from the pioneering work on small molecule mimics in the late 1970s, we have assisted to a
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