Based on the the UV-Vis, RR spectra, EPR spectra and MD simulations of the mutated proteins,the OH- anion builds three H-bonds at alkaline pH, with TrpG8, TyrCD1 and with a water molecule H-bonded to TyrB10. Therefore, the OH- ligand appears to be the only example of involvement of TyrB10 -albeit an indirect one- in the stabilization of the exogenous ligand. In the present work the data obtained for different anionic ligands will be compared and discussed in terms of the different capability of the TyrB10 and TyrCD1 to act as hydrogen bond donor or acceptor.
The role of the distal tyrosines in the H-bonding stabilization of the exogeneous ligands in Thermobifida fusca hemoglobin / Francesco P. Nicoletti; Enrica Droghetti; Barry D. Howes; Juan P. Bustamante; Alessandra Bonamore; Natascia Sciamanna; Darío A. Estrin; Alessandro Feis; Alberto Boffi; Giulietta Smulevich. - ELETTRONICO. - (2014), pp. 355-355. (Intervento presentato al convegno Eight international conference of porphyrins and Phtalocyanines (ICPP-8) tenutosi a Istanbul, Turchia nel June 22-27, 2014).