Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Marcos N, Morgada"'
Autor:
Cat McCann, Michael Quinteros, Ifeoluwa Adelugba, Marcos N. Morgada, Aida R. Castelblanco, Emily J. Davis, Antonio Lanzirotti, Sarah J. Hainer, Alejandro J. Vila, Juan G. Navea, Teresita Padilla-Benavides
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The loading of copper (Cu) into cytochrome c oxidase (COX) in mitochondria is essential for energy production in cells. Extensive studies have been performed to characterize mitochondrial cuproenzymes that contribute to the metallation of COX, such a
Externí odkaz:
https://doaj.org/article/68efc8fe18604b64aa27dc185ae288ff
Autor:
Shivatheja Soma, Marcos N. Morgada, Mandar T. Naik, Aren Boulet, Anna A. Roesler, Nathaniel Dziuba, Alok Ghosh, Qinhong Yu, Paul A. Lindahl, James B. Ames, Scot C. Leary, Alejandro J. Vila, Vishal M. Gohil
Publikováno v:
Cell Reports, Vol 29, Iss 12, Pp 4114-4126.e5 (2019)
Summary: In eukaryotes, cellular respiration is driven by mitochondrial cytochrome c oxidase (CcO), an enzyme complex that requires copper cofactors for its catalytic activity. Insertion of copper into its catalytically active subunits, including COX
Externí odkaz:
https://doaj.org/article/6322aed5c16a4dc79ccf348a0f9dc969
Autor:
Cat, McCann, Michael, Quinteros, Ifeoluwa, Adelugba, Marcos N, Morgada, Aida R, Castelblanco, Emily J, Davis, Antonio, Lanzirotti, Sarah J, Hainer, Alejandro J, Vila, Juan G, Navea, Teresita, Padilla-Benavides
Publikováno v:
Frontiers in molecular biosciences. 9
The loading of copper (Cu) into cytochrome c oxidase (COX) in mitochondria is essential for energy production in cells. Extensive studies have been performed to characterize mitochondrial cuproenzymes that contribute to the metallation of COX, such a
Autor:
Florencia Emiliani, Damián Alvarez-Paggi, Luciano A. Abriata, Alejandro J. Vila, Kelly N. Chacón, Daniel H. Murgida, Marcos N. Morgada, Ninian J. Blackburn
Publikováno v:
Inorganic Chemistry. 58:15687-15691
CuA centers perform efficient long-range electron transfer. The electronic structure of native CuA sites can be described by a double-potential well with a dominant σu* ground state in fast equilibrium with a less populated πu ground state. Here, w
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
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
Publikováno v:
Metal ions in life sciences. 20
CuA is a binuclear copper center acting as an electron transfer hub in terminal oxidases such as cytochrome c oxidase and nitrous oxide reductase. Its unique electronic structure is intimately linked to its function and has puzzled the community of b
Autor:
Alejandro J. Vila, Maria Ana Castro, Alcides J. Leguto, Jonathan Szuster, Ulises A. Zitare, Daniel H. Murgida, Marcos N. Morgada
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new or improved redox functions. Here we report that implantation of ligand loops from natural T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef68105bdb8b43b320f1771474a1047e
http://pubs.rsc.org/en/Content/ArticleLanding/2020/SC/D0SC01620A
http://pubs.rsc.org/en/Content/ArticleLanding/2020/SC/D0SC01620A
CuA is a binuclear copper center acting as an electron transfer hub in terminal oxidases such as cytochrome c oxidase and nitrous oxide reductase. Its unique electronic structure is intimately linked to its function and has puzzled the community of b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bced63f2e70e7a20638192ed2ca72f66
https://doi.org/10.1515/9783110589757-010
https://doi.org/10.1515/9783110589757-010
Autor:
María-Natalia Lisa, Marcos N. Morgada, Pedro M. Alzari, Alejandro J. Vila, Estefanía Giannini, María-Eugenia Llases
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, Wiley, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
FEBS Journal, 2020, 287 (4), pp.749-762. ⟨10.1111/febs.15016⟩
International audience; The assembly of the CuA site in Cytochrome c Oxidase (COX) is a critical step for aerobic respiration in COX-dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c348181ad2f281e82d06082a2669053
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095808
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095808
Autor:
Alejandro J. Vila, Daniel H. Murgida, María-Eugenia Llases, Estefanía Giannini, María-Natalia Lisa, Marcos N. Morgada, María A. Castro, Pedro M. Alzari
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemical Communications, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
Chemical Communications, Royal Society of Chemistry, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Chemical Communications, 2020, 56 (8), pp.1223-1226. ⟨10.1039/c9cc08883k⟩
The CuA center is a paradigm for the study of long-range biological electron transfer. This metal center is an essential cofactor for terminal oxidases like cytochrome c oxidase, the enzymatic complex responsible for cellular respiration in eukaryote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4b6c8756d542e6078ac4e28a120fe3
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095789
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095789