Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin
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 hydro...
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todo:paper_00062960_v53_n51_p8021_Nicoletti2023-10-03T14:04:34Z Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin Nicoletti, F.P. Bustamante, J.P. Droghetti, E. Howes, B.D. Fittipaldi, M. Bonamore, A. Baiocco, P. Feis, A. Boffi, A. Estrin, D.A. Smulevich, G. bacterial protein heme ligand recombinant protein truncated hemoglobin Actinomycetales binding site chemical structure chemistry electron spin resonance genetics hydrogen bond metabolism molecular dynamics pH protein stability Raman spectrometry site directed mutagenesis Actinomycetales Bacterial Proteins Binding Sites Electron Spin Resonance Spectroscopy Heme Hydrogen Bonding Hydrogen-Ion Concentration Ligands Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Protein Stability Recombinant Proteins Spectrum Analysis, Raman Truncated Hemoglobins 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. (Chemical Equation Presented). © 2014 American Chemical Society. Fil:Bustamante, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v53_n51_p8021_Nicoletti |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
bacterial protein heme ligand recombinant protein truncated hemoglobin Actinomycetales binding site chemical structure chemistry electron spin resonance genetics hydrogen bond metabolism molecular dynamics pH protein stability Raman spectrometry site directed mutagenesis Actinomycetales Bacterial Proteins Binding Sites Electron Spin Resonance Spectroscopy Heme Hydrogen Bonding Hydrogen-Ion Concentration Ligands Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Protein Stability Recombinant Proteins Spectrum Analysis, Raman Truncated Hemoglobins |
| spellingShingle |
bacterial protein heme ligand recombinant protein truncated hemoglobin Actinomycetales binding site chemical structure chemistry electron spin resonance genetics hydrogen bond metabolism molecular dynamics pH protein stability Raman spectrometry site directed mutagenesis Actinomycetales Bacterial Proteins Binding Sites Electron Spin Resonance Spectroscopy Heme Hydrogen Bonding Hydrogen-Ion Concentration Ligands Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Protein Stability Recombinant Proteins Spectrum Analysis, Raman Truncated Hemoglobins Nicoletti, F.P. Bustamante, J.P. Droghetti, E. Howes, B.D. Fittipaldi, M. Bonamore, A. Baiocco, P. Feis, A. Boffi, A. Estrin, D.A. Smulevich, G. Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| topic_facet |
bacterial protein heme ligand recombinant protein truncated hemoglobin Actinomycetales binding site chemical structure chemistry electron spin resonance genetics hydrogen bond metabolism molecular dynamics pH protein stability Raman spectrometry site directed mutagenesis Actinomycetales Bacterial Proteins Binding Sites Electron Spin Resonance Spectroscopy Heme Hydrogen Bonding Hydrogen-Ion Concentration Ligands Models, Molecular Molecular Dynamics Simulation Mutagenesis, Site-Directed Protein Stability Recombinant Proteins Spectrum Analysis, Raman Truncated Hemoglobins |
| description |
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. (Chemical Equation Presented). © 2014 American Chemical Society. |
| format |
JOUR |
| author |
Nicoletti, F.P. Bustamante, J.P. Droghetti, E. Howes, B.D. Fittipaldi, M. Bonamore, A. Baiocco, P. Feis, A. Boffi, A. Estrin, D.A. Smulevich, G. |
| author_facet |
Nicoletti, F.P. Bustamante, J.P. Droghetti, E. Howes, B.D. Fittipaldi, M. Bonamore, A. Baiocco, P. Feis, A. Boffi, A. Estrin, D.A. Smulevich, G. |
| author_sort |
Nicoletti, F.P. |
| title |
Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| title_short |
Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| title_full |
Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| title_fullStr |
Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| title_full_unstemmed |
Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
| title_sort |
interplay of the h-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of thermobifida fusca truncated hemoglobin |
| url |
http://hdl.handle.net/20.500.12110/paper_00062960_v53_n51_p8021_Nicoletti |
| work_keys_str_mv |
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