Artículo

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" (2014) Biochemistry. 53(51):8021-8030
El editor solo permite decargar el artículo en su versión post-print desde el repositorio. Por favor, si usted posee dicha versión, enviela a
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

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
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
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
Volumen:53
Número:51
Página de inicio:8021
Página de fin:8030
DOI: http://dx.doi.org/10.1021/bi501132a
Título revista:Biochemistry
Título revista abreviado:Biochemistry
ISSN:00062960
CODEN:BICHA
CAS:heme, 14875-96-8; Bacterial Proteins; Heme; Ligands; Recombinant Proteins; Truncated Hemoglobins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v53_n51_p8021_Nicoletti

Referencias:

  • Capece, L., Boechi, L., Perissinotti, L.L., Arroyo-Mañez, P., Bikiel, D.E., Smulevich, G., Marti, M.A., Estrin, D.A., Small ligand-globin interactions: Reviewing lessons derived from computer simulation (2013) Biochim. Biophys. Acta, 1834, pp. 1722-1738
  • Bonamore, A., Ilari, A., Giangiacomo, L., Bellelli, A., Morea, V., Boffi, A., A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca (2005) FEBS J., 272, pp. 4189-4201
  • Droghetti, E., Nicoletti, F.P., Bonamore, A., Boechi, L., Arroyo-Mañez, P., Estrin, D.A., Boffi, A., Feis, A., Hemepocket structural properties of a bacterial truncated hemoglobin from Thermobifida fusca (2010) Biochemistry, 49, pp. 10394-10402
  • Droghetti, E., Nicoletti, F.P., Bonamore, A., Sciamanna, N., Boffi, A., Feis, A., Smulevich, G., The optical spectra of fluoride complexes can effectively probe H-bonding interactions in the distal cavity of heme proteins (2011) J. Inorg. Biochem., 105, pp. 1338-1343
  • Nicoletti, F.P., Droghetti, E., Boechi, L., Bonamore, A., Sciamanna, N., Estrin, D.A., Feis, A., Smulevich, G., Fluoride as a probe for H-bonding interactions in the active site of heme proteins: The case of Thermobifida f usca hemoglobin (2011) J. Am. Chem. Soc., 133, pp. 20970-20980
  • Nicoletti, F.P., Comandini, A., Bonamore, A., Boechi, L., Boubeta, F.M., Feis, A., Smulevich, G., Boffi, A., Sulfide binding properties of truncated hemoglobins (2010) Biochemistry, 49, pp. 2269-2278
  • Nicoletti, F.P., Droghetti, E., Howes, B.D., Bustamante, J.P., Bonamore, A., Sciamanna, N., Estrin, D.A., Smulevich, G., H-bonding networks of the distal residues and water molecules in the active site of Thermobif ida f usca hemoglobin (2013) Biochim. Biophys. Acta, 1834, pp. 1901-1909
  • Feis, A., Marzocchi, M.P., Smulevich, G., Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures (1994) Biochemistry, 33, pp. 4577-4583
  • Asher, S.A., Vickery, L.E., Schuster, T.M., Sauer, K., Resonance Raman spectra of methemoglobin derivatives. Selective enhancement of axial ligand vibrations and lack of an effect of inositol hexaphosphate (1977) Biochemistry, 16, pp. 5849-5856
  • Asher, S.A., Schuster, T.M., Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives (1979) Biochemistry, 18, pp. 5377-5387
  • Egawa, T., Yeh, S.-R.J., Structural and functional properties of hemoglobins (2005) Inorg. Biochem., 99, pp. 72-96
  • Ikeda-Saito, M., Hori, H., Andersson, L.A., Prince, R.C., Pickering, I.J., George, G.N., Sanders, C.R., Mattera, R., Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants (1992) J. Biol. Chem., 267, pp. 22843-22852
  • Lukat-Rodgers, G.S., Rodgers, K.R., Spin-state equilibria and axial ligand bonding in FixL hydroxide: A resonance Raman study (1998) J. Biol. Inorg. Chem., 3, pp. 274-281
  • Brunori, M., Amiconi, G., Antonin, E., Wyman, J., Zito, R., Fanelli, A.R., The transition between 'acid' and 'alkaline' ferric heme proteins (1968) Biochim. Biophys. Acta, 154, pp. 315-322
  • Palmer, G., The electron paramagnetic resonance of metalloproteins (1985) Biochem. Soc. Trans., 13, pp. 548-560
  • Hagen, W.R., Dislocation strain broadening as a source of anisotropic linewidth and asymmetrical lineshape in the electron paramagnetic resonance spectrum of metalloproteins and related systems (1981) J. Magn. Reson., 44, pp. 447-469
  • Taylor, C.P.S., The EPR of low spin heme complexes. Relation of the t2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters (1977) Biochim. Biophys. Acta, 491, pp. 137-149
  • Howes, B.D., Feis, A., Indiani, C., Marzocchi, M.P., Smulevich, G., Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature (2000) J. Biol. Inorg. Chem., 5, pp. 227-235
  • Kraus, D.W., Wittenberg, J.B., Lu, J.F., Peisach, J., Hemoglobins of the Lucina pectinata/bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins (1990) J. Biol. Chem., 265, pp. 16054-16059
  • Izadi, N., Henry, Y., Haladjian, J., Goldberg, M.E., Wandersman, C., Delepierre, M., Lecroisey, A., Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition (1997) Biochemistry, 36, pp. 7050-7057
  • Arnoux, P., Haser, R., Izadi, N., Lecroisey, A., Delepierre, M., Wandersman, C., Czjzek, M., The crystal structure of HasA, a hemophore secreted by Serratia marcescens (1999) Nat. Struct. Biol., 6, pp. 516-520
  • Nicoletti, F.P., Howes, B.D., Fittipaldi, M., Fanali, G., Fasano, M., Ascenzi, P., Smulevich, G., Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation (2008) J. Am. Chem. Soc., 130, pp. 11677-11688
  • Blumberg, W.E., Peisach, J., Probes of enzymes and hemoproteins (1971) Probes of Structure and Function of Macromolecules and Membranes, pp. 215-228. , Yonetani, T., Mildvan, A. S., and Chance, B., Eds. Academic Press, New York
  • Brautigan, D.L., Feinberg, B.A., Hoffman, B.M., Margoliash, E., Peisach, J., Blumberg, W.E., Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c (1977) J. Biol. Chem., 252, pp. 574-582
  • Walker, F.A., Huynh, B.H., Scheidt, W.R., Osvath, S.R., Models of the cytochromes b. Effect of axial ligand plane orientation on the EPR and Moessbauer spectra of low-spin ferrihemes (1986) J. Am. Chem. Soc., 108, pp. 5288-5297
  • Ascenzi, P., Di Masi, A., Tundo, G.R., Pesce, A., Visca, P., Coletta, M., Nitrosylation mechanisms of Mycobacterium tuberculosis and Campylobacter jejuni truncated hemoglobins N, O, and P (2014) PLoS One, 9, p. e102811

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