A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media
The selectivity of MnIII/II porphyrinates toward nitroxyl or nitric oxide donors provides a convenient starting point for the development of new materials for the speciation of these nitrogen-containing redox relatives. In the present report, we describe the insertion of MnIII protoporphyrinate IX i...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01620134_v105_n8_p1044_Boron http://hdl.handle.net/20.500.12110/paper_01620134_v105_n8_p1044_Boron |
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paper:paper_01620134_v105_n8_p1044_Boron2023-06-08T15:13:34Z A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media Suarez, Sebastian Doctorovich, Fabio Ariel Martí, Marcelo Adrián Bari, Sara Elizabeth Nitric oxide Nitroxyl Reconstituted apomyoglobin Speciation apomyoglobin manganese nitric acid derivative nitric oxide aerobic capacity anaerobic capacity article chemical reaction chemical reaction kinetics controlled study culture medium decomposition molecular mechanics spectral sensitivity spectroscopy The selectivity of MnIII/II porphyrinates toward nitroxyl or nitric oxide donors provides a convenient starting point for the development of new materials for the speciation of these nitrogen-containing redox relatives. In the present report, we describe the insertion of MnIII protoporphyrinate IX in apomyoglobin and its chemical behavior toward HNO or NO donors, either under anaerobic or aerobic conditions. For comparison and discussion, the MnIII porphyrinate, devoid of the protein matrix, was studied in parallel. The MnIII reconstituted globin successfully reacted with the nitroxyl donor trioxodinitrate, while it was unreactive toward NO or NO donors, in good agreement with previously reported data on water soluble MnIII porphyrinates. The estimated association rate constant for the reaction with the nitroxyl donor was of the same order of magnitude for the reconstituted globin and the free porphyrinate, suggesting that the protein environment is not involved in the reaction mechanism. In contrast, the reaction product exhibited enhanced stability in the presence of dioxygen only when the porphyrinate was included in the protein matrix; this feature is ascribed to the role of the distal residues on the metal centered reactivity. This behavior is required for spectroscopic detection under biologically relevant conditions. © 2011 Elsevier Inc. Fil:Suárez, S.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Doctorovich, F. 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:Bari, S.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2011 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01620134_v105_n8_p1044_Boron http://hdl.handle.net/20.500.12110/paper_01620134_v105_n8_p1044_Boron |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Nitric oxide Nitroxyl Reconstituted apomyoglobin Speciation apomyoglobin manganese nitric acid derivative nitric oxide aerobic capacity anaerobic capacity article chemical reaction chemical reaction kinetics controlled study culture medium decomposition molecular mechanics spectral sensitivity spectroscopy |
spellingShingle |
Nitric oxide Nitroxyl Reconstituted apomyoglobin Speciation apomyoglobin manganese nitric acid derivative nitric oxide aerobic capacity anaerobic capacity article chemical reaction chemical reaction kinetics controlled study culture medium decomposition molecular mechanics spectral sensitivity spectroscopy Suarez, Sebastian Doctorovich, Fabio Ariel Martí, Marcelo Adrián Bari, Sara Elizabeth A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
topic_facet |
Nitric oxide Nitroxyl Reconstituted apomyoglobin Speciation apomyoglobin manganese nitric acid derivative nitric oxide aerobic capacity anaerobic capacity article chemical reaction chemical reaction kinetics controlled study culture medium decomposition molecular mechanics spectral sensitivity spectroscopy |
description |
The selectivity of MnIII/II porphyrinates toward nitroxyl or nitric oxide donors provides a convenient starting point for the development of new materials for the speciation of these nitrogen-containing redox relatives. In the present report, we describe the insertion of MnIII protoporphyrinate IX in apomyoglobin and its chemical behavior toward HNO or NO donors, either under anaerobic or aerobic conditions. For comparison and discussion, the MnIII porphyrinate, devoid of the protein matrix, was studied in parallel. The MnIII reconstituted globin successfully reacted with the nitroxyl donor trioxodinitrate, while it was unreactive toward NO or NO donors, in good agreement with previously reported data on water soluble MnIII porphyrinates. The estimated association rate constant for the reaction with the nitroxyl donor was of the same order of magnitude for the reconstituted globin and the free porphyrinate, suggesting that the protein environment is not involved in the reaction mechanism. In contrast, the reaction product exhibited enhanced stability in the presence of dioxygen only when the porphyrinate was included in the protein matrix; this feature is ascribed to the role of the distal residues on the metal centered reactivity. This behavior is required for spectroscopic detection under biologically relevant conditions. © 2011 Elsevier Inc. |
author |
Suarez, Sebastian Doctorovich, Fabio Ariel Martí, Marcelo Adrián Bari, Sara Elizabeth |
author_facet |
Suarez, Sebastian Doctorovich, Fabio Ariel Martí, Marcelo Adrián Bari, Sara Elizabeth |
author_sort |
Suarez, Sebastian |
title |
A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
title_short |
A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
title_full |
A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
title_fullStr |
A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
title_full_unstemmed |
A protective protein matrix improves the discrimination of nitroxyl from nitric oxide by MnIII protoporphyrinate IX in aerobic media |
title_sort |
protective protein matrix improves the discrimination of nitroxyl from nitric oxide by mniii protoporphyrinate ix in aerobic media |
publishDate |
2011 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01620134_v105_n8_p1044_Boron http://hdl.handle.net/20.500.12110/paper_01620134_v105_n8_p1044_Boron |
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