A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties
Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. F...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00062960_v46_n37_p10733_Todorovic |
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todo:paper_00062960_v46_n37_p10733_Todorovic2023-10-03T14:04:25Z A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties Todorovic, S. Leal, S.S. Salgueiro, C.A. Zebger, I. Hildebrandt, P. Murgida, D.H. Gomes, C.M. Cofactors Metalloproteins Secondary structure Thermal perturbation Chemical modification Conformations Iron Perturbation techniques Raman spectroscopy Sulfur Proteins ferredoxin iron sulfur Acidianus Acidianus ambivalens alpha helix article conformational transition electron spin resonance infrared spectroscopy low temperature nonhuman priority journal protein conformation protein folding protein secondary structure Raman spectrometry structure analysis temperature sensitivity Acidianus Circular Dichroism Cysteine Ferredoxins Iron-Sulfur Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Protein Folding Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared Temperature Transition Temperature Acidianus ambivalens Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of α-helical content at relatively low temperatures (Tm app ∼ 44°C), followed by the disruption of both iron-sulfur clusters (Tm app sim; 53-60°C). The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T m app ∼ 58°C) and a change, rather than a significant net loss, of secondary structure (Tm app ∼ 60°C). This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors. © 2007 American Chemical Society. Fil:Murgida, D.H. 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_00062960_v46_n37_p10733_Todorovic |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Cofactors Metalloproteins Secondary structure Thermal perturbation Chemical modification Conformations Iron Perturbation techniques Raman spectroscopy Sulfur Proteins ferredoxin iron sulfur Acidianus Acidianus ambivalens alpha helix article conformational transition electron spin resonance infrared spectroscopy low temperature nonhuman priority journal protein conformation protein folding protein secondary structure Raman spectrometry structure analysis temperature sensitivity Acidianus Circular Dichroism Cysteine Ferredoxins Iron-Sulfur Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Protein Folding Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared Temperature Transition Temperature Acidianus ambivalens |
| spellingShingle |
Cofactors Metalloproteins Secondary structure Thermal perturbation Chemical modification Conformations Iron Perturbation techniques Raman spectroscopy Sulfur Proteins ferredoxin iron sulfur Acidianus Acidianus ambivalens alpha helix article conformational transition electron spin resonance infrared spectroscopy low temperature nonhuman priority journal protein conformation protein folding protein secondary structure Raman spectrometry structure analysis temperature sensitivity Acidianus Circular Dichroism Cysteine Ferredoxins Iron-Sulfur Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Protein Folding Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared Temperature Transition Temperature Acidianus ambivalens Todorovic, S. Leal, S.S. Salgueiro, C.A. Zebger, I. Hildebrandt, P. Murgida, D.H. Gomes, C.M. A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| topic_facet |
Cofactors Metalloproteins Secondary structure Thermal perturbation Chemical modification Conformations Iron Perturbation techniques Raman spectroscopy Sulfur Proteins ferredoxin iron sulfur Acidianus Acidianus ambivalens alpha helix article conformational transition electron spin resonance infrared spectroscopy low temperature nonhuman priority journal protein conformation protein folding protein secondary structure Raman spectrometry structure analysis temperature sensitivity Acidianus Circular Dichroism Cysteine Ferredoxins Iron-Sulfur Proteins Ligands Magnetic Resonance Spectroscopy Models, Molecular Protein Folding Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared Temperature Transition Temperature Acidianus ambivalens |
| description |
Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of α-helical content at relatively low temperatures (Tm app ∼ 44°C), followed by the disruption of both iron-sulfur clusters (Tm app sim; 53-60°C). The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T m app ∼ 58°C) and a change, rather than a significant net loss, of secondary structure (Tm app ∼ 60°C). This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors. © 2007 American Chemical Society. |
| format |
JOUR |
| author |
Todorovic, S. Leal, S.S. Salgueiro, C.A. Zebger, I. Hildebrandt, P. Murgida, D.H. Gomes, C.M. |
| author_facet |
Todorovic, S. Leal, S.S. Salgueiro, C.A. Zebger, I. Hildebrandt, P. Murgida, D.H. Gomes, C.M. |
| author_sort |
Todorovic, S. |
| title |
A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| title_short |
A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| title_full |
A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| title_fullStr |
A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| title_full_unstemmed |
A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| title_sort |
spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties |
| url |
http://hdl.handle.net/20.500.12110/paper_00062960_v46_n37_p10733_Todorovic |
| work_keys_str_mv |
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