The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties. (Articolo in rivista)

Type

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

Label

• The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1074/jbc.M407267200 (literal)

Alternative label

• Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E. (2005)
  The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties.
  in The Journal of biological chemistry (Print)
  (literal)

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

• Giangiacomo L, Ilari A, Boffi A, Morea V, Chiancone E. (literal)

Pagina inizio

• 9192 (literal)

Pagina fine

• 9202 (literal)

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

• 280 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, Dept Biochem Sci, I-00185 Rome, Italy (literal)

Titolo

• The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties. (literal)

Abstract

• The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed, purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein endowed with an unusually high oxygen affinity ( in the nanomolar range) such that the apparent thermodynamic binding constant for O-2 exceeds that for CO by 1 order of magnitude. The kinetic basis of the high oxygen affinity resides mainly in the very slow rate of ligand release. The extremely stable ferrous oxygenated adduct is resistant to oxidation, which can be achieved only with oxidant in large excess, e. g. ferricyanide in 50-fold molar excess. The three-dimensional crystal structure of the cyano-Met derivative was determined at 2.15 Angstrom resolution. Although the overall fold resembles that of other truncated hemoglobins, the distal heme pocket displays a unique array of hydrophilic side chains in the topological positions that dominate the steric interaction with iron-bound ligands. In fact, the Tyr-B10, Thr-E7, and Gln-E11 oxygens on one side of the heme pocket and the Trp-G8 indole NE1 nitrogen on the other form a novel pattern of the \"ligand-inclusive hydrogen bond network\" described for mycobacterial HbO. On the proximal side, the histidine residue is in an unstrained conformation, and the iron-His bond is unusually short ( 1.91 Angstrom). (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

• EMILIA CHIANCONE (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)
• ALBERTO BOFFI (Unità di personale esterno)
• VERONICA MOREA (Unità di personale interno)

Insieme di parole chiave

• Keywords of "The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties." (Insieme di parole chiave)

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

• EMILIA CHIANCONE (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)
• VERONICA MOREA (Unità di personale interno)
• ALBERTO BOFFI (Unità di personale esterno)

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

• ?The ?Journal of biological chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties." (Insieme di parole chiave)