Structural studies on flavohemoglobins. (Articolo in rivista)

Type
Label
  • Structural studies on flavohemoglobins. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0076-6879(08)36010-8 (literal)
Alternative label
  • Ilari A, Boffi A. (2008)
    Structural studies on flavohemoglobins.
    in Methods in enzymology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ilari A, Boffi A. (literal)
Pagina inizio
  • 187 (literal)
Pagina fine
  • 202 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 436 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, Rome, Italy 2. Univ Roma La Sapienza, Dept Biochem Sci, Rome, Italy (literal)
Titolo
  • Structural studies on flavohemoglobins. (literal)
Abstract
  • The key three-dimensional features of flavohemoglobins have been unveiled by X-ray crystallographic investigations carried out on the Alcaligenes eutrophus and Escherichia coli proteins. Flavohemoglobins are made of a globin domain fused with a ferredoxin reductase-like FAD binding module and display highly conserved sequences in the active sites of both the heme-binding domain and the flavin-binding domain. Structural studies are discussed and methodological approaches to the solution of the crystal structures and to the analysis of the relevant stereochemical properties of the active sites are presented. The understanding of the structural properties of flavohemoglobins serves as a guide for testing biological hypotheses and allows for a rational evaluation of structure-based alignments within the flavohemoglobin family. (literal)
Prodotto di
Autore CNR

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