Výsledky vyhledávání - "Magali F. Scocozza"

Akademický článek

Loops around the Heme Pocket Have a Critical Role in the Function and Stability of BsDyP from Bacillus subtilis

Autor: Carolina F. Rodrigues, Patrícia T. Borges, Magali F. Scocozza, Diogo Silva, André Taborda, Vânia Brissos, Carlos Frazão, Lígia O. Martins

Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 19, p 10862 (2021)

Bacillus subtilis BsDyP belongs to class I of the dye-decolorizing peroxidase (DyP) family of enzymes and is an interesting biocatalyst due to its high redox potential, broad substrate spectrum and thermostability. This work reports the optimization

Externí odkaz: https://doaj.org/article/ea01b241b4894e1bbf04b0a77b07fc3d

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Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases

Autor: Magali F. Scocozza, Lígia O. Martins, Daniel H. Murgida

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 22
International Journal of Molecular Sciences, Vol 22, Iss 12532, p 12532 (2021)

This work introduces a novel way to obtain catalytically competent oxyferryl species for two different dye-decolorizing peroxidases (DyPs) in the absence of H2O2 or any other peroxide by simply applying a reductive electrochemical potential under aer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c16d185552cf4e7c541d0759cc2a40b6

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Autor: Santiago Oviedo-Rouco, Cecilia Spedalieri, Daniel H. Murgida, Florencia Tomasina, Verónica Tórtora, Magali F. Scocozza, Rafael Radi

Publikováno v: Bioelectrochemistry (Amsterdam, Netherlands). 143

Cytochrome c (Cyt c) is a multifunctional protein that, in its native conformation, shuttles electrons in the mitochondrial respiratory chain. Conformational transitions that involve replacement of the heme distal ligand lead to the gain of alternati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72238aa61d06c32c85b11643255ac263
https://pubmed.ncbi.nlm.nih.gov/34624727

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The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions

Autor: Alcides J. Leguto, Ulises A. Zitare, Daniel H. Murgida, Marcos N. Morgada, Jonathan Szuster, Magali F. Scocozza, Alejandro J. Vila, Andrés Espinoza-Cara

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

Here we report the effect of molecular crowding on long-range protein electron transfer (ET) and disentangle the specific responses of the redox site and the protein milieu. To this end, we studied two different one-electron redox proteins that share

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89b2b0a7005cba51f6a01a0ff500374f
https://doi.org/10.1016/j.electacta.2018.10.069

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