Artículo

Nicoletti, F.P.; Droghetti, E.; Howes, B.D.; Bustamante, J.P.; Bonamore, A.; Sciamanna, N.; Estrin, D.A.; Feis, A.; Boffi, A.; Smulevich, G. "H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin" (2013) Biochimica et Biophysica Acta - Proteins and Proteomics. 1834(9):1901-1909
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Abstract:

The ferric form of truncated hemoglobin II from Thermobifida fusca (Tf-trHb) and its triple mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN- have been characterized by resonance Raman spectroscopy, electron paramagnetic resonance spectroscopy, and molecular dynamics simulations. Tf-trHb contains three polar residuesin the distal site, namely TrpG8, TyrCD1 and TyrB10. Whereas TrpG8 can act as a potential hydrogen-bond donor, the tyrosines can act as donors or acceptors. Ligand binding in heme-containing proteins is determined by a number of factors, including the nature and conformation of the distal residues and their capability to stabilize the heme-bound ligand via hydrogen-bonding and electrostatic interactions. Since both the RR Fe-OH- and Fe-CN - frequencies are very sensitive to the distal environment, detailed information on structural variations has been obtained. The hydroxyl ligand binds only the WT protein giving rise to two different conformers. In form 1 the anion is stabilized by H-bonds with TrpG8, TyrCD1 and a water molecule, inturn H-bonded to TyrB10. In form 2, H-bonding with TyrCD1 is mediated by a water molecule. Unlike the OH- ligand, CN- binds both WT and the triple mutant giving rise to two forms with similar spectroscopic characteristics. The overall results clearly indicate that H-bonding interactions both with distal residues and water molecules are important structural determinants in the active site of Tf-trHb. This article is part of a Special Issue entitled: Oxygen Binding and Sensing Proteins. © 2013 Elsevier B.V. All rights reserved.

Registro:

Documento: Artículo
Título:H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
Autor:Nicoletti, F.P.; Droghetti, E.; Howes, B.D.; Bustamante, J.P.; Bonamore, A.; Sciamanna, N.; Estrin, D.A.; Feis, A.; Boffi, A.; Smulevich, G.
Filiación:Dipartimento di Chimica Ugo Schiff, Università di Firenze, Via della Lastruccia 3-13, I-50019 Sesto Fiorentino (FI), Italy
Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellon II, Buenos Aires C1428EHA, Argentina
Department of Biochemical Sciences and CNR, Institute of Molecular Biology and Pathology, University of Rome La Sapienza, Piazzale Aldo Moro 5, I-00185 Rome, Italy
Palabras clave:Cyanide ligand; Hydrogen-bond; Hydroxyl ligand; Resonance Raman; Truncated hemoglobin; cyanide; hydroxyl group; ligand; truncated hemoglobin; tyrosine; water; cyanide; heme; hemoglobin; hydroxide; hydroxide ion; myoglobin; truncated hemoglobin; alkalinity; article; electron spin resonance; hydrogen bond; ligand binding; molecular dynamics; molecule; nonhuman; priority journal; Raman spectrometry; static electricity; Thermobifida fusca; 2-(N-morpholino)ethanesulfonic acid; 5c; 6c; acidic surface variant of Tf-trHb containing two single site mutations Phe107Glu and Arg91Glu; Actinomycetales; ASV; Cyanide ligand; enzyme active site; five-coordinate; genetics; high spin; HS; hydrogen bond; Hydrogen-bond; Hydroxyl ligand; low spin; LS; Mb; MD; MES; metabolism; pH; protein binding; Resonance Raman; RR; six-coordinate; Tf; Thermobifida fusca; trHb; wild type; WT; Thermobifida fusca; 2-(N-morpholino)ethanesulfonic acid; 5c; 6c; acidic surface variant of Tf-trHb containing two single site mutations Phe107Glu and Arg91Glu; ASV; Cyanide ligand; electron paramagnetic resonance; EPR; five-coordinate; Hb; hemoglobin; high spin; HS; Hydrogen-bond; Hydroxyl ligand; low spin; LS; Mb; MD; MES; molecular dynamics; myoglobin; Resonance Raman; resonance Raman; RR; six-coordinate; Tf; Thermobifida fusca; trHb; truncated hemoglobin; Truncated hemoglobin; wild type; WT; Actinomycetales; Catalytic Domain; Cyanides; Heme; Hemoglobins; Hydrogen Bonding; Hydrogen-Ion Concentration; Hydroxides; Molecular Dynamics Simulation; Protein Binding; Spectrum Analysis, Raman; Tyrosine; Water
Año:2013
Volumen:1834
Número:9
Página de inicio:1901
Página de fin:1909
DOI: http://dx.doi.org/10.1016/j.bbapap.2013.02.033
Título revista:Biochimica et Biophysica Acta - Proteins and Proteomics
Título revista abreviado:Biochim. Biophys. Acta Proteins Proteomics
ISSN:15709639
CODEN:BBAPB
CAS:cyanide, 57-12-5; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; water, 7732-18-5; heme, 14875-96-8; hemoglobin, 9008-02-0; hydroxide, 14280-30-9; Cyanides; Heme, 14875-96-8; Hemoglobins; Hydroxides; Tyrosine, 55520-40-6; Water, 7732-18-5; hydroxide ion, 9159UV381P
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15709639_v1834_n9_p1901_Nicoletti

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Citas:

---------- APA ----------
Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., Estrin, D.A.,..., Smulevich, G. (2013) . H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin. Biochimica et Biophysica Acta - Proteins and Proteomics, 1834(9), 1901-1909.
http://dx.doi.org/10.1016/j.bbapap.2013.02.033
---------- CHICAGO ----------
Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., et al. "H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin" . Biochimica et Biophysica Acta - Proteins and Proteomics 1834, no. 9 (2013) : 1901-1909.
http://dx.doi.org/10.1016/j.bbapap.2013.02.033
---------- MLA ----------
Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., et al. "H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin" . Biochimica et Biophysica Acta - Proteins and Proteomics, vol. 1834, no. 9, 2013, pp. 1901-1909.
http://dx.doi.org/10.1016/j.bbapap.2013.02.033
---------- VANCOUVER ----------
Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., et al. H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin. Biochim. Biophys. Acta Proteins Proteomics. 2013;1834(9):1901-1909.
http://dx.doi.org/10.1016/j.bbapap.2013.02.033