We have exploited the availability of a combinatorial set of mutants, in each of which these three amino acids have been singly, doubly, or triply replaced by a Phe residue, to investigate the H-bonding interactions between the distal protein aminoacids with the F- and OH- anionic ligands bound to the heme iron.
Binding of anionic ligands in the active site of the bacterial hemoglobin from Thermobifida fusca / Francesco P. Nicoletti; Enrica Droghetti; Leonardo Boechi; Natascia Sciamanna; Juan Pablo Bustamante; Alessandra Bonamore; Dario A. Estrin; Alberto Boffi; Alessandro Feis; Giulietta Smulevich. - ELETTRONICO. - (2012), pp. 192-192. (Intervento presentato al convegno Seventh International Conference on Porphyrins and Phthalocyanines tenutosi a Jeju, Giappone nel 1-6 luglio 2012).
Binding of anionic ligands in the active site of the bacterial hemoglobin from Thermobifida fusca
NICOLETTI, FRANCESCO PAOLO;DROGHETTI, ENRICA;FEIS, ALESSANDRO;SMULEVICH, GIULIETTA
2012
Abstract
We have exploited the availability of a combinatorial set of mutants, in each of which these three amino acids have been singly, doubly, or triply replaced by a Phe residue, to investigate the H-bonding interactions between the distal protein aminoacids with the F- and OH- anionic ligands bound to the heme iron.
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