Azanone (HNO) interaction with Hemeproteins and metalloporphyrins
Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are o...
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2012
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08988838_v64_n_p97_Doctorovich http://hdl.handle.net/20.500.12110/paper_08988838_v64_n_p97_Doctorovich |
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paper:paper_08988838_v64_n_p97_Doctorovich2023-06-08T15:49:28Z Azanone (HNO) interaction with Hemeproteins and metalloporphyrins Doctorovich, Fabio Ariel Bikiel, Damian Ezequiel Pellegrino, Juan Suarez, Sebastian Martí, Marcelo Adrián Azanone Cobalt Heme HNO Iron Kinetics Manganese Myoglobin Nitrosyl Nitroxyl Nitroxyl anion NO NOS Oxidation Porphyrin Protein Reductive nitrosylation Ruthenium Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are observed. Due to its high reactivity, azanone studies rely on the use of donors, molecules that therefore offer interesting therapeutic perspectives. In this review, we firstly describe the pharmacological potential of azanone, the chemistry of the available donors, and the main biological relevant HNO reactions with special focus on heme proteins and metalloporphyrins (Fe, Mn, and Co). Finally, we present evidence concerning the endogenous . in vivo azanone production hypothesis, and how the recent porphyrin-based developed methods for its detection may contribute to solve this key physiological question. © 2012 Elsevier Inc. Fil:Doctorovich, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Bikiel, D.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pellegrino, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Suárez, S.A. 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. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08988838_v64_n_p97_Doctorovich http://hdl.handle.net/20.500.12110/paper_08988838_v64_n_p97_Doctorovich |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Azanone Cobalt Heme HNO Iron Kinetics Manganese Myoglobin Nitrosyl Nitroxyl Nitroxyl anion NO NOS Oxidation Porphyrin Protein Reductive nitrosylation Ruthenium |
| spellingShingle |
Azanone Cobalt Heme HNO Iron Kinetics Manganese Myoglobin Nitrosyl Nitroxyl Nitroxyl anion NO NOS Oxidation Porphyrin Protein Reductive nitrosylation Ruthenium Doctorovich, Fabio Ariel Bikiel, Damian Ezequiel Pellegrino, Juan Suarez, Sebastian Martí, Marcelo Adrián Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| topic_facet |
Azanone Cobalt Heme HNO Iron Kinetics Manganese Myoglobin Nitrosyl Nitroxyl Nitroxyl anion NO NOS Oxidation Porphyrin Protein Reductive nitrosylation Ruthenium |
| description |
Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are observed. Due to its high reactivity, azanone studies rely on the use of donors, molecules that therefore offer interesting therapeutic perspectives. In this review, we firstly describe the pharmacological potential of azanone, the chemistry of the available donors, and the main biological relevant HNO reactions with special focus on heme proteins and metalloporphyrins (Fe, Mn, and Co). Finally, we present evidence concerning the endogenous . in vivo azanone production hypothesis, and how the recent porphyrin-based developed methods for its detection may contribute to solve this key physiological question. © 2012 Elsevier Inc. |
| author |
Doctorovich, Fabio Ariel Bikiel, Damian Ezequiel Pellegrino, Juan Suarez, Sebastian Martí, Marcelo Adrián |
| author_facet |
Doctorovich, Fabio Ariel Bikiel, Damian Ezequiel Pellegrino, Juan Suarez, Sebastian Martí, Marcelo Adrián |
| author_sort |
Doctorovich, Fabio Ariel |
| title |
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| title_short |
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| title_full |
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| title_fullStr |
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| title_full_unstemmed |
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins |
| title_sort |
azanone (hno) interaction with hemeproteins and metalloporphyrins |
| publishDate |
2012 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08988838_v64_n_p97_Doctorovich http://hdl.handle.net/20.500.12110/paper_08988838_v64_n_p97_Doctorovich |
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