Sulfide binding properties of truncated hemoglobins

The truncated hemoglobins from Bacillus subtilis (Bs-trHb) and Thermobifida fusca (Tf-trHb) have been shown to form high-affinity complexes with hydrogen sulfide in their ferric state. The recombinant proteins, as extracted, from Escherichia coli cells after overexpression, are indeed partially satu...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Nicoletti, F.P., Comandini, A., Bonamore, A., Boechi, L., Boubeta, F.M., Feis, A., Smulevich, I., Boffi, A.
Formato:	JOUR
Materias:	Bacillus Subtilis Bearing-only Binding parameter Binding properties Bound ligands Classical molecular dynamics Cysteine biosynthesis Escherichia coli cells Experimental data Ferric iron High affinity Hydrogen bonding stabilization Kinetic barrier Kinetic study Lucina pectinata Order of magnitude Over-expression Partially saturated Recombinant protein Resonance Raman spectroscopy Second-order rate constants Stretching bands Sulfide species Thermobifida fusca Truncated hemoglobins Wild-type proteins Bacteriology Binding energy Biochemistry Coordination reactions Escherichia coli Hemoglobin Hydrogen Hydrogen bonds Molecular dynamics Raman spectroscopy Rate constants Spin dynamics Stabilization Sulfur determination Hydrogen sulfide bacterial protein cysteine ferric ion hydrogen sulfide recombinant protein truncated hemoglobin article Bacillus subtilis bacterial cell bacterium binding affinity biosynthesis homeostasis hydrogen bond kinetics molecular dynamics nonhuman point mutation priority journal protein analysis Raman spectrometry thermodynamics Actinomycetales Bacterial Proteins Kinetics Molecular Dynamics Simulation Protein Binding Protein Conformation Spectrophotometry, Ultraviolet Sulfides Thermodynamics Truncated Hemoglobins
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00062960_v49_n10_p2269_Nicoletti
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

Ejemplares similares

Sulfide binding properties of truncated hemoglobins
Publicado: (2010)

Unraveling the molecular basis for ligand binding in truncated hemoglobins: The trHbO Bacillus subtilis case
por: Boechi, Leonardo, et al.
Publicado: (2010)

Unraveling the molecular basis for ligand binding in truncated hemoglobins: The trHbO Bacillus subtilis case
por: Boechi, L., et al.

Heme pocket structural properties of a bacterial truncated hemoglobin from thermobifida fusca
Publicado: (2010)

Heme pocket structural properties of a bacterial truncated hemoglobin from thermobifida fusca
por: Droghetti, E., et al.

Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
por: Bustamante, Juan Pablo, et al.
Publicado: (2012)

Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
por: Marcelli, A., et al.
Publicado: (2012)

Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
por: Marcelli, A., et al.

Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca
por: Marcelli, A., et al.
Publicado: (2012)

Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni
Publicado: (2011)

Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from campylobacter jejuni
por: Arroyo Mañez, P., et al.

Molecular basis of thermal stability in truncated (2/2) hemoglobins
por: Bustamante, Juan Pablo, et al.
Publicado: (2014)

Molecular basis of thermal stability in truncated (2/2) hemoglobins
por: Bustamante, J.P., et al.

Fluoride as a probe for h-bonding interactions in the active site of heme proteins: The case of thermobifida fusca hemoglobin
Publicado: (2011)

Fluoride as a probe for h-bonding interactions in the active site of heme proteins: The case of thermobifida fusca hemoglobin
por: Nicoletti, F.P., et al.

Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin
por: Bustamante, Juan Pablo, et al.
Publicado: (2014)

Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin
por: Nicoletti, F.P., et al.

Reactivity of inorganic sulfide species toward a heme protein model
por: Boubeta, Fernando Martin, et al.
Publicado: (2015)

Reactivity of inorganic sulfide species toward a heme protein model
por: Bieza, S.A., et al.

Access and Binding of H2S to Hemeproteins: The Case of HbI of Lucina pectinata
por: Boubeta, Fernando Martin, et al.
Publicado: (2016)

Access and Binding of H2S to Hemeproteins: The Case of HbI of Lucina pectinata
por: Boubeta, F.M., et al.

Ligand uptake modulation by internal water molecules and hydrophobic cavities in hemoglobins
por: Bustamante, Juan Pablo, et al.
Publicado: (2014)

Ligand uptake modulation by internal water molecules and hydrophobic cavities in hemoglobins
por: Bustamante, J.P., et al.

Cold-Adaptation Signatures in the Ligand Rebinding Kinetics to the Truncated Hemoglobin of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125
Publicado: (2018)

Cold-Adaptation Signatures in the Ligand Rebinding Kinetics to the Truncated Hemoglobin of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125
por: Boubeta, F.M., et al.

Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from Thermobifida fusca HbO
Publicado: (2015)

Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from Thermobifida fusca HbO
por: Howes, B.D., et al.

H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
por: Bustamante, Juan Pablo, et al.
Publicado: (2013)

H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
por: Nicoletti, F.P., et al.

Mechanism of Sulfide Binding by Ferric Hemeproteins
Publicado: (2018)

Mechanism of Sulfide Binding by Ferric Hemeproteins
por: Boubeta, F.M., et al.

The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin
por: Ferreiro, Dardo N., et al.
Publicado: (2013)

The key role of water in the dioxygenase function of Escherichia coli flavohemoglobin
por: Ferreiro, D.N., et al.

The N-terminal pre-A region of Mycobacterium tuberculosis 2/2HbN promotes NO-dioxygenase activity
por: Bustamante, Juan Pablo, et al.
Publicado: (2016)

The N-terminal pre-A region of Mycobacterium tuberculosis 2/2HbN promotes NO-dioxygenase activity
por: Pesce, A., et al.

Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
por: Martí, Marcelo Adrián, et al.
Publicado: (2007)

Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases
por: Martí, M.A., et al.

Structural Plasticity in Globins: Role of Protein Dynamics in Defining Ligand Migration Pathways
por: Capece, Luciana, et al.
Publicado: (2016)

Structural Plasticity in Globins: Role of Protein Dynamics in Defining Ligand Migration Pathways
por: Estarellas, C., et al.

Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O
por: Boechi, Leonardo, et al.
Publicado: (2008)