Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin. (Articolo in rivista)

Type

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

Label

• Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin. (Articolo in rivista) (literal)

Anno

• 2007-01-01T00:00:00+01:00 (literal)

Alternative label

• Vicente JB; Scandurra FM; Rodrigues JV; Brunori M; Sarti P; Teixeira M; Giuffrè A. (2007)
  Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin.
  in The FEBS journal (Print)
  (literal)

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

• Vicente JB; Scandurra FM; Rodrigues JV; Brunori M; Sarti P; Teixeira M; Giuffrè A. (literal)

Pagina inizio

• 677 (literal)

Pagina fine

• 686 (literal)

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

• 274 (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Instituto de Tecnologia Qu?´mica e Biolo´ gica, Universidade Nova de Lisboa, Oeiras, Portugal; Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology and Istituto Pasteur - Fondazione Cenci Bolognetti, University of Rome 'La Sapienza', Italy. (literal)

Titolo

• Kinetics of electron transfer from NADH to the Escherichia coli nitric oxide reductase flavorubredoxin. (literal)

Abstract

• Escherichia coli flavorubredoxin (FlRd) belongs to the family of flavodiiron proteins (FDPs), microbial enzymes that are expressed to scavenge nitric oxide (NO) under anaerobic conditions. To degrade NO, FlRd has to be reduced by NADH via the FAD-binding protein flavorubredoxin reductase, thus the kinetics of electron transfer along this pathway was investigated by stopped-flow absorption spectroscopy. We found that NADH, but not NADPH, quickly reduces the FlRd-reductase (k ¼ 5.5 ± 2.2 · 106 m)1Æs)1 at 5 ?C), with a limiting rate of 255 ± 17 s)1. The reductase in turn quickly reduces the rubredoxin (Rd) center of FlRd, as assessed at 5 ?C working with the native FlRd enzyme (k ¼ 2.4 ± 0.1 · 106 m)1Æs)1) and with its isolated Rd-domain (k ? 1 · 107 m)1Æs)1); in both cases the reaction was found to be dependent on pH and ionic strength. In FlRd the fast reduction of the Rd center occurs synchronously with the formation of flavin mononucleotide semiquinone. Our data provide evidence that (a) FlRd-reductase rapidly shuttles electrons between NADH and FlRd, a prerequisite for NO reduction in this detoxification pathway, and (b) the electron accepting site in FlRd, the Rd center, is in very fast redox equilibrium with the flavin mononucleotide. (literal)

Prodotto di

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

Autore CNR

• MAURIZIO BRUNORI (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)
• MAURIZIO BRUNORI (Persona)

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

• ?The ?FEBS journal (Rivista)