http://www.cnr.it/ontology/cnr/individuo/prodotto/ID244159
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)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Federici, L ; Savino, C ; Musto, R; Travaglini-Allocatelli, C; Cutruzzola, F; Brunori, M (literal)
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- 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)
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