EngineeringHis (E7) affects the control of heme reactivity in Aplysia limacina myoglobin (Articolo in rivista)

Type
Label
  • EngineeringHis (E7) affects the control of heme reactivity in Aplysia limacina myoglobin (Articolo in rivista) (literal)
Anno
  • 2000-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1006/bbrc.2000.2259 (literal)
Alternative label
  • Federici, L ; Savino, C ; Musto, R; Travaglini-Allocatelli, C; Cutruzzola, F; Brunori, M (2000)
    EngineeringHis (E7) affects the control of heme reactivity in Aplysia limacina myoglobin
    in Biochemical and biophysical research communications (Print); Elsevier - Academic Press Inc., San Diego (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Federici, L ; Savino, C ; Musto, R; Travaglini-Allocatelli, C; Cutruzzola, F; Brunori, M (literal)
Pagina inizio
  • 58 (literal)
Pagina fine
  • 63 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 269 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [ 1 ] Univ Rome La Sapienza, Dept Biochem Sci A Rossi Fanelli, I-00185 Rome, Italy [ 2 ] Univ Rome La Sapienza, CNR, Ctr Mol Biol, I-00185 Rome, Italy (literal)
Titolo
  • EngineeringHis (E7) affects the control of heme reactivity in Aplysia limacina myoglobin (literal)
Abstract
  • Aplysia limacina myoglobin lacks the distal histidine (His (E7)) and displays a ligand stabilization mechanism based on Arg(E10). The double mutant Val(E7)His-Arg(E10)Thr has been prepared to engineer the role of His(E7), typical of mammalian myoglobins, in a different globin framework. The 2.0 Angstrom crystal structure of Val(E7)His-Arg(E10)Thr met-Mb mutant reveals that the His(E7) side chain points out of the distal pocket, providing an explanation for the observed failure to stabilize the Fe(II) bound oxygen in the ferrous myoglobin. Moreover, spectroscopic analysis together with kinetic data on azide binding to met-myoglobin are reported and discussed in terms of the presence of a water molecule at coordination distance from the heme iron (literal)
Editore
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Editore di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it