The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125
The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 α-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic para...
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todo:paper_09498257_v16_n2_p299_Howes2023-10-03T15:49:36Z The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 Howes, B.D. Giordano, D. Boechi, L. Russo, R. Mucciacciaro, S. Ciaccio, C. Sinibaldi, F. Fittipaldi, M. Martí, M.A. Estrin, D.A. Di Prisco, G. Coletta, M. Verde, C. Smulevich, G. Antarctic bacterium EPR Molecular dynamics Resonance Raman Tyrosinate ligand bacterial protein hemoglobin protein TAC125 tryptophan tyrosine unclassified drug article Bacillus subtilis cold acclimatization controlled study crystal structure gene overexpression gene sequence Geobacillus stearothermophilus molecular cloning molecular dynamics Mycobacterium tuberculosis nonhuman oxidation reduction potential priority journal protein analysis protein purification protein structure Pseudoalteromonas Pseudoalteromonas haloplanktis Raman spectrometry sequence alignment Shewanella oneidensis simulation Bacterial Proteins Electrochemistry Electron Spin Resonance Spectroscopy Hemoglobins Molecular Dynamics Simulation Oxidation-Reduction Pseudoalteromonas Temperature Bacteria (microorganisms) Pseudoalteromonas haloplanktis The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 α-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands. © 2010 SBIC. Fil:Boechi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Martí, M.A. 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_09498257_v16_n2_p299_Howes |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Antarctic bacterium EPR Molecular dynamics Resonance Raman Tyrosinate ligand bacterial protein hemoglobin protein TAC125 tryptophan tyrosine unclassified drug article Bacillus subtilis cold acclimatization controlled study crystal structure gene overexpression gene sequence Geobacillus stearothermophilus molecular cloning molecular dynamics Mycobacterium tuberculosis nonhuman oxidation reduction potential priority journal protein analysis protein purification protein structure Pseudoalteromonas Pseudoalteromonas haloplanktis Raman spectrometry sequence alignment Shewanella oneidensis simulation Bacterial Proteins Electrochemistry Electron Spin Resonance Spectroscopy Hemoglobins Molecular Dynamics Simulation Oxidation-Reduction Pseudoalteromonas Temperature Bacteria (microorganisms) Pseudoalteromonas haloplanktis |
| spellingShingle |
Antarctic bacterium EPR Molecular dynamics Resonance Raman Tyrosinate ligand bacterial protein hemoglobin protein TAC125 tryptophan tyrosine unclassified drug article Bacillus subtilis cold acclimatization controlled study crystal structure gene overexpression gene sequence Geobacillus stearothermophilus molecular cloning molecular dynamics Mycobacterium tuberculosis nonhuman oxidation reduction potential priority journal protein analysis protein purification protein structure Pseudoalteromonas Pseudoalteromonas haloplanktis Raman spectrometry sequence alignment Shewanella oneidensis simulation Bacterial Proteins Electrochemistry Electron Spin Resonance Spectroscopy Hemoglobins Molecular Dynamics Simulation Oxidation-Reduction Pseudoalteromonas Temperature Bacteria (microorganisms) Pseudoalteromonas haloplanktis Howes, B.D. Giordano, D. Boechi, L. Russo, R. Mucciacciaro, S. Ciaccio, C. Sinibaldi, F. Fittipaldi, M. Martí, M.A. Estrin, D.A. Di Prisco, G. Coletta, M. Verde, C. Smulevich, G. The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| topic_facet |
Antarctic bacterium EPR Molecular dynamics Resonance Raman Tyrosinate ligand bacterial protein hemoglobin protein TAC125 tryptophan tyrosine unclassified drug article Bacillus subtilis cold acclimatization controlled study crystal structure gene overexpression gene sequence Geobacillus stearothermophilus molecular cloning molecular dynamics Mycobacterium tuberculosis nonhuman oxidation reduction potential priority journal protein analysis protein purification protein structure Pseudoalteromonas Pseudoalteromonas haloplanktis Raman spectrometry sequence alignment Shewanella oneidensis simulation Bacterial Proteins Electrochemistry Electron Spin Resonance Spectroscopy Hemoglobins Molecular Dynamics Simulation Oxidation-Reduction Pseudoalteromonas Temperature Bacteria (microorganisms) Pseudoalteromonas haloplanktis |
| description |
The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 α-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands. © 2010 SBIC. |
| format |
JOUR |
| author |
Howes, B.D. Giordano, D. Boechi, L. Russo, R. Mucciacciaro, S. Ciaccio, C. Sinibaldi, F. Fittipaldi, M. Martí, M.A. Estrin, D.A. Di Prisco, G. Coletta, M. Verde, C. Smulevich, G. |
| author_facet |
Howes, B.D. Giordano, D. Boechi, L. Russo, R. Mucciacciaro, S. Ciaccio, C. Sinibaldi, F. Fittipaldi, M. Martí, M.A. Estrin, D.A. Di Prisco, G. Coletta, M. Verde, C. Smulevich, G. |
| author_sort |
Howes, B.D. |
| title |
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| title_short |
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| title_full |
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| title_fullStr |
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| title_full_unstemmed |
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 |
| title_sort |
peculiar heme pocket of the 2/2 hemoglobin of cold-adapted pseudoalteromonas haloplanktis tac125 |
| url |
http://hdl.handle.net/20.500.12110/paper_09498257_v16_n2_p299_Howes |
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