Abstract:
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.
Registro:
Documento: |
Artículo
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Título: | Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin |
Autor: | 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. |
Filiación: | Dipartimento di Chimica Ugo Schiff, Università di Firenze, Via della Lastruccia 3-13, Sesto Fiorentino (FI), I-50019, Italy Departamento de Quimica Inorganica, Analitica y Quimica Fisica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EHA, Argentina INSTM, Dipartimento di Fisica e Astronomia, Università degli Studi di Firenze, via Sansone 1, Sesto Fiorentino, I-50019, Italy Institute Pasteur, Department of Biochemical Sciences, University of Rome la Sapienza, Piazzale Aldo Moro 5, Rome, I-00185, Italy Center of Life Nano Sciences, Italian Institute of Technology, Viale Regina Elena 291, Rome, I-00161, Italy Sanofi, Viale Bodio 37, Milano, I-20158, Italy
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Palabras clave: | 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 |
Año: | 2014
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Volumen: | 53
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Número: | 51
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Página de inicio: | 8021
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Página de fin: | 8030
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DOI: |
http://dx.doi.org/10.1021/bi501132a |
Título revista: | Biochemistry
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Título revista abreviado: | Biochemistry
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ISSN: | 00062960
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CODEN: | BICHA
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CAS: | heme, 14875-96-8; Bacterial Proteins; Heme; Ligands; Recombinant Proteins; Truncated Hemoglobins
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v53_n51_p8021_Nicoletti |
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Citas:
---------- APA ----------
Nicoletti, F.P., Bustamante, J.P., Droghetti, E., Howes, B.D., Fittipaldi, M., Bonamore, A., Baiocco, P.,..., Smulevich, G.
(2014)
. Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin. Biochemistry, 53(51), 8021-8030.
http://dx.doi.org/10.1021/bi501132a---------- CHICAGO ----------
Nicoletti, F.P., Bustamante, J.P., Droghetti, E., Howes, B.D., Fittipaldi, M., Bonamore, A., et al.
"Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin"
. Biochemistry 53, no. 51
(2014) : 8021-8030.
http://dx.doi.org/10.1021/bi501132a---------- MLA ----------
Nicoletti, F.P., Bustamante, J.P., Droghetti, E., Howes, B.D., Fittipaldi, M., Bonamore, A., et al.
"Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin"
. Biochemistry, vol. 53, no. 51, 2014, pp. 8021-8030.
http://dx.doi.org/10.1021/bi501132a---------- VANCOUVER ----------
Nicoletti, F.P., Bustamante, J.P., Droghetti, E., Howes, B.D., Fittipaldi, M., Bonamore, A., et al. Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin. Biochemistry. 2014;53(51):8021-8030.
http://dx.doi.org/10.1021/bi501132a