INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
Interplay of the H-bond donor-acceptor role by distal residues in the hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin
NICOLETTI, FRANCESCO P.; BUSTAMANTE, JUAN PABLO; DROGHETTI, ENRICA; HOWES, BARRY D.; FITTIPALDI, MARIA; BONAMORE, ALESSANDRA; BAIOCCO, PAOLA; FEIS, ALESSANDRO; BOFFI, ALBERTO; ESTRIN, DARÍO; SMULEVICH, GIULIETTA
AMER CHEMICAL SOC
Lugar: Washington; Año: 2014 p. 8021 - 8021
The unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal amino acids. The behavior of the heme-bound hydroxyl, in particular, has generated much interest in view of the relationships between the spin-state equilibrium of the ferric iron atom and hydrogen-bonding capabilities (as either acceptor or donor) of the OH− group itself. The present investigation offers a detailed molecular dynamics and spectroscopic picture of the hydroxyl complexes of the WT protein and a combinatorial set of mutants, in which the distal polar residues, TrpG8, TyrCD1, and TyrB10, have been singly, doubly, or triply replaced by a Phe residue. Each mutant is characterized by a complex interplay of interactions in which the hydroxyl ligand may act both as a H-bond donor or acceptor. The resonance Raman stretching frequencies of the Fe−OH moiety, together with electron paramagnetic resonance spectra and MD simulations on each mutant, have enabled the identification of specific contributions to the unique ligand-inclusive H-bond network typical of this globin family.