Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Carlos D, Brondino"'
Publikováno v:
Journal of Magnetic Resonance Open, Vol 16, Iss , Pp 100117- (2023)
Transition metal ion-containing oxidoreductases, which carry out long-distance electron transfer reactions, are a large family of metalloproteins that are widely distributed in nature. The metal ions are either present as mononuclear centers or are o
Externí odkaz:
https://doaj.org/article/2e9d213f4bd4481387200787e8aaf3d8
Autor:
Alberto Claudio Rizzi, Carlos A. Ramos, Carlos D. Brondino, Ricardo Baggio, Axel Kemmerer, Ana Laura Pérez, Sergio D. Dalosto, Mario Cesar Guillermo Passeggi
Publikováno v:
European Journal of Inorganic Chemistry. 2021:4183-4195
Autor:
Ayelén F. Crespi, Paula N. Zomero, Verónica M. Sánchez, Ana L. Pérez, Carlos D. Brondino, Daniel Vega, Enrique Rodríguez‐Castellón, Juan M. Lázaro‐Martínez
Publikováno v:
ChemPlusChem. 87
Autor:
Alberto Claudio Rizzi, Julio César Cristaldi, Carlos D. Brondino, Pablo J. González, Sergio D. Dalosto, Maria G. Rivas, Felix Martín Ferroni, Cintia S. Ramírez, Andrea Belén Duré
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Two domain copper-nitrite reductases (NirK) contain two types of copper centers, one electron transfer (ET) center of type 1 (T1) and a catalytic site of type 2 (T2). NirK activity is pH-dependent, which has been suggested to be produced by structura
Autor:
Alberto Claudio Rizzi, Pablo J. González, Maria G. Rivas, Carlos D. Brondino, Felix Martín Ferroni
Publikováno v:
Science Reviews - from the end of the world. 1:6-23
Oxidoreductases containing transition metal ions are widespread in nature and are essential for living organisms. The copper-containing nitrite reductase (NirK) and the molybdenum-containing aldehyde oxidoreductase (Aor) are typical examples of oxido
Autor:
Andrea B. Duré, Julio C. Cristaldi, Lorieth A. Guevara Cuasapud, Sergio D. Dalosto, María Gabriela Rivas, Felix M. Ferroni, Pablo J. González, Guillermo G. Montich, Carlos D. Brondino
Publikováno v:
SSRN Electronic Journal.
Autor:
Maria G. Rivas, Pablo J. González, Diederik J. Opperman, Carlos D. Brondino, Carmien Tolmie, Felix Martín Ferroni, Cintia S. Ramírez
Publikováno v:
Protein Sci
We report the crystal structure of the copper-containing nitrite reductase (NirK) from the Gram-negative bacterium Sinorhizobium meliloti 2011 (Sm), together with complex structural alignment and docking studies with both non-cognate and the physiolo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7201413bc4eb7eace3da62530ef1c878
https://europepmc.org/articles/PMC8521279/
https://europepmc.org/articles/PMC8521279/
Autor:
Ayelén F, Crespi, Verónica M, Sánchez, Daniel, Vega, Ana L, Pérez, Carlos D, Brondino, Yamila Garro, Linck, Paul, Hodgkinson, Enrique, Rodríguez-Castellón, Juan M, Lázaro-Martínez
Publikováno v:
RSC advances. 11(33)
The complex chemical functionalization of aldehyde moieties in Cu(ii)- and Co(ii)-pyridinecarboxaldehyde complexes was studied. X-ray studies demonstrated that the aldehyde group (R
Autor:
Jacopo Marangon, Hugo D Correia, Carlos D Brondino, José J G Moura, Maria J Romão, Pablo J González, Teresa Santos-Silva
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83234 (2013)
Mononuclear Mo-containing enzymes of the xanthine oxidase (XO) family catalyze the oxidative hydroxylation of aldehydes and heterocyclic compounds. The molybdenum active site shows a distorted square-pyramidal geometry in which two ligands, a hydroxy
Externí odkaz:
https://doaj.org/article/87f6f1b5c1bf4da4b70f5488b2ceaeb8
Autor:
Julio C, Cristaldi, Felix M, Ferroni, Andrea B, Duré, Cintia S, Ramírez, Sergio D, Dalosto, Alberto C, Rizzi, Pablo J, González, Maria G, Rivas, Carlos D, Brondino
Publikováno v:
Metallomics : integrated biometal science. 12(12)
Two domain copper-nitrite reductases (NirK) contain two types of copper centers, one electron transfer (ET) center of type 1 (T1) and a catalytic site of type 2 (T2). NirK activity is pH-dependent, which has been suggested to be produced by structura