Nanohybrid Assemblies of Porphyrin and Au10 Cluster Nanoparticles

Autor: Mariachiara Trapani, Maria Angela Castriciano, Andrea Romeo, Giovanna De Luca, Nelson Machado, Barry D. Howes, Giulietta Smulevich, Luigi Monsù Scolaro

Publikováno v: Nanomaterials, Vol 9, Iss 7, p 1026 (2019)

The interaction between gold sub-nanometer clusters composed of ten atoms (Au10) and tetrakis(4-sulfonatophenyl)porphyrin (TPPS) was investigated through various spectroscopic techniques. Under mild acidic conditions, the formation, in aqueous soluti

Externí odkaz: https://doaj.org/article/0c24b33506924395ba5dcdebe5fe85bc

Study of manganese binding to the ferroxidase centre of human H-type ferritin

Autor: M. Lantieri, Emilia Chiancone, Silvia Sottini, Maria Fittipaldi, Annarita Fiorillo, Barry D. Howes, Gabriele Spina, Elisabetta Falvo, Donella Rovai, Simonetta Stefanini, Andrea Ilari, Dante Gatteschi, Matteo Ardini

Publikováno v: Journal of inorganic biochemistry 182 (2018): 103–112. doi:10.1016/j.jinorgbio.2018.02.003
info:cnr-pdr/source/autori:Ardini M.; Howes B.D.; Fiorillo A.; Falvo E.; Sottini S.; Rovai D.; Lantieri M.; Ilari A.; Gatteschi D.; Spina G.; Chiancone E.; Stefanini S.; Fittipaldi M./titolo:Study of manganese binding to the ferroxidase centre of human H-type ferritin/doi:10.1016%2Fj.jinorgbio.2018.02.003/rivista:Journal of inorganic biochemistry/anno:2018/pagina_da:103/pagina_a:112/intervallo_pagine:103–112/volume:182

Ferritins are ubiquitous and conserved proteins endowed with enzymatic ferroxidase activity, that oxidize Fe(II) ions at the dimetal ferroxidase centre to form a mineralized Fe(III) oxide core deposited within the apo-protein shell. Herein, the in vi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b506ebd3f9aeb70377af59a28088bb1d
https://doi.org/10.1016/j.jinorgbio.2018.02.003

The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein.

Autor: Clara Iannuzzi, Salvatore Adinolfi, Barry D Howes, Ricardo Garcia-Serres, Martin Clémancey, Jean-Marc Latour, Giulietta Smulevich, Annalisa Pastore

Publikováno v: PLoS ONE, Vol 6, Iss 7, p e21992 (2011)

Progress in understanding the mechanism underlying the enzymatic formation of iron-sulfur clusters is difficult since it involves a complex reaction and a multi-component system. By exploiting different spectroscopies, we characterize the effect on t

Externí odkaz: https://doaj.org/article/9c7c7a5b48d64bd99d6ea4af5b056c54

Nanohybrid Assemblies of Porphyrin and Au10 Cluster Nanoparticles

Autor: Luigi Monsù Scolaro, Giulietta Smulevich, Andrea Romeo, Nelson Machado, Maria Angela Castriciano, Mariachiara Trapani, Barry D. Howes, Giovanna De Luca

Publikováno v: Nanomaterials
Volume 9
Issue 7
Nanomaterials (Basel) 9 (2019). doi:10.3390/nano9071026
info:cnr-pdr/source/autori:Trapani, Mariachiara; Castriciano, Maria Angela; Romeo, Andrea; De Luca, Giovanna; Machado, Nelson; Howes, Barry D.; Smulevich, Giulietta; Scolaro, Luigi Monsu/titolo:Nanohybrid Assemblies of Porphyrin and Au-10 Cluster Nanoparticles/doi:10.3390%2Fnano9071026/rivista:Nanomaterials (Basel)/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
Nanomaterials, Vol 9, Iss 7, p 1026 (2019)

The interaction between gold sub-nanometer clusters composed of ten atoms (Au10) and tetrakis(4-sulfonatophenyl)porphyrin (TPPS) was investigated through various spectroscopic techniques. Under mild acidic conditions, the formation, in aqueous soluti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68504c906f3694f1f81fcb606505ee55

Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes

Autor: Lisa, Milazzo, Stefan, Hofbauer, Barry D, Howes, Thomas, Gabler, Paul G, Furtmüller, Christian, Obinger, Giulietta, Smulevich

Publikováno v: Biochemistry

Coproheme decarboxylases (ChdC) catalyze the hydrogen peroxide-mediated conversion of coproheme to heme b. This work compares the structure and function of wild-type (WT) coproheme decarboxylase from Listeria monocytogenes and its M149A, Q187A, and M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b9674bec838b4519cb8d9495d3289cbe
https://pubmed.ncbi.nlm.nih.gov/29536725