Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state. (Articolo in rivista)

Type
Label
  • Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Artali R.; Marchini N.; Meneghetti F.; Cavazzini D.; Cassetta A.; Sassone C. (2005)
    Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state.
    in Acta crystallographica. Section D (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Artali R.; Marchini N.; Meneghetti F.; Cavazzini D.; Cassetta A.; Sassone C. (literal)
Pagina inizio
  • 481 (literal)
Pagina fine
  • 484 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 61 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
  • PubMe (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Artali R. -Institute of Pharmaceutical Chemistry, University of Milano Marchini N. -Institute of Pharmaceutical Chemistry, University of Milano Meneghetti F. -Institute of Pharmaceutical Chemistry, University of Milano Cavazzini D. -Department of Biochemistry and Molecular Biology, University of Parma Cassetta A. -IC-CNR, Trieste Sassone C. -Department of Human and Animal Biology, University of Torino (literal)
Titolo
  • Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state. (literal)
Abstract
  • The crystallographic structure of an engineered flavodoxin mutant from Desulfovibrio vulgaris has been analysed. Site-directed mutagenesis was used to substitute serine 35 with a cysteine to provide a possible covalent linkage. The crystal structure of the semiquinone form of this mutant is similar to the corresponding oxidation state of the wild-type flavodoxin. Analysis of the structural changes reveals the interaction between N(5)H of the flavin and the carbonyl O atom of Gly61 to be critical for modulation of the electrochemical properties of the protein. (literal)
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