The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status (Articolo in rivista)

Type

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

Label

• The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

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

• 10.1111/j.1742-4658.2008.06775.x (literal)

Alternative label

• Giancaspero TA; Locato V; de Pinto MC;De Gara L; Barile M. (2009)
  The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status
  in The FEBS journal (Print)
  (literal)

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

• Giancaspero TA; Locato V; de Pinto MC;De Gara L; Barile M. (literal)

Pagina inizio

• 219 (literal)

Pagina fine

• 231 (literal)

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

• 276 (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Univ Bari, Dipartimento Biochim & Biol Mol E Quagliariello, I-70126 Bari, Italy (literal)

Titolo

• The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status (literal)

Abstract

• Intact mitochondria isolated from Nicotiana tabacum cv. Bright Yellow 2 (TBY-2) cells can take up riboflavin via carrier-mediated systems that operate at different concentration ranges and have different uptake efficiencies. Once inside mitochondria, riboflavin is converted into catalytically active cofactors, FMN and FAD, due to the existence of a mitochondrial riboflavin kinase (EC 2.7.1.26) and an FAD synthetase (EC 2.7.7.2). Newly synthesized FAD can be exported from intact mitochondria via a putative FAD exporter. The dependence of FMN synthesis rate on riboflavin concentration shows saturation kinetics with a sigmoidal shape (S(0.5), V(max) and Hill coefficient values 0.32 +/- 0.12 mu m, 1.4 nmol.min(-1).mg(-1) protein and 3.1, respectively). The FAD-forming enzymes are both activated by MgCl(2), and reside in two distinct monofunctional enzymes, which can be physically separated in mitochondrial soluble and membrane-enriched fractions, respectively. (literal)

Prodotto di

• Interrelazione nucleo/citoplasma/mitocondri nell'omeostasi cellulare. (SV.P15.003.001) (Modulo)
• Istituto di biomembrane e bioenergetica (IBBE) (Istituto)

Autore CNR

• MARIA BARILE (Persona)

Insieme di parole chiave

• Parole chiave di "The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status" (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto di biomembrane e bioenergetica (IBBE) (Istituto)
• Interrelazione nucleo/citoplasma/mitocondri nell'omeostasi cellulare. (SV.P15.003.001) (Modulo)

Autore CNR di

• MARIA BARILE (Persona)

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

• ?The ?FEBS journal (Rivista)

Insieme di parole chiave di

• Parole chiave di "The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status" (Insieme di parole chiave)