Flavodiiron Oxygen Reductase from Entamoeba histolytica MODULATION OF SUBSTRATE PREFERENCE BY TYROSINE 271 AND LYSINE 53 (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Flavodiiron Oxygen Reductase from Entamoeba histolytica MODULATION OF SUBSTRATE PREFERENCE BY TYROSINE 271 AND LYSINE 53 (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1074/jbc.M114.579086 (literal)

Alternative label

• Goncalves, Vera L.; Vicente, Joao B.; Pinto, Liliana; Romao, Celia V.; Frazao, Carlos; Sarti, Paolo; Giuffre, Alessandro; Teixeira, Miguel (2014)
  Flavodiiron Oxygen Reductase from Entamoeba histolytica MODULATION OF SUBSTRATE PREFERENCE BY TYROSINE 271 AND LYSINE 53
  in The Journal of biological chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Goncalves, Vera L.; Vicente, Joao B.; Pinto, Liliana; Romao, Celia V.; Frazao, Carlos; Sarti, Paolo; Giuffre, Alessandro; Teixeira, Miguel (literal)

Pagina inizio

• 28260 (literal)

Pagina fine

• 28270 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 289 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 11 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 41 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Universidade Nova de Lisboa; Universidade de Lisboa; Universidade de Lisboa; Sapienza University Rome; Sapienza University Rome; Consiglio Nazionale delle Ricerche (CNR) (literal)

Titolo

• Flavodiiron Oxygen Reductase from Entamoeba histolytica MODULATION OF SUBSTRATE PREFERENCE BY TYROSINE 271 AND LYSINE 53 (literal)

Abstract

• Flavodiiron proteins (FDPs) are a family of enzymes endowed with bona fide oxygen- and/or nitric-oxide reductase activity, although their substrate specificity determinants remain elusive. After a comprehensive comparison of available three-dimensional structures, particularly of FDPs with a clear preference toward either O-2 or NO, two main differences were identified near the diiron active site, which led to the construction of site-directed mutants of Tyr(271) and Lys(53) in the oxygen reducing Entamoeba histolytica EhFdp1. The biochemical and biophysical properties of these mutants were studied by UV-visible and electron paramagnetic resonance (EPR) spectroscopies coupled to potentiometry. Their reactivity with O-2 and NO was analyzed by stopped-flow absorption spectroscopy and amperometric methods. These mutations, whereas keeping the overall properties of the redox cofactors, resulted in increased NO reductase activity and faster inactivation of the enzyme in the reaction with O-2, pointing to a role of the mutated residues in substrate selectivity. (literal)

Prodotto di

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR

• PAOLO SARTI (Persona)
• ALESSANDRO GIUFFRE' (Unità di personale interno)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• ALESSANDRO GIUFFRE' (Unità di personale interno)
• PAOLO SARTI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?Journal of biological chemistry (Rivista)