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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Autores principales: Doctorovich, F., Bikiel, D.E., Pellegrino, J., Suárez, S.A., Martí, M.A.
Formato: SER
Materias:
HNO
NO
NOS
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_08988838_v64_n_p97_Doctorovich
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spelling todo:paper_08988838_v64_n_p97_Doctorovich2023-10-03T15:44:04Z Azanone (HNO) interaction with Hemeproteins and metalloporphyrins Doctorovich, F. Bikiel, D.E. Pellegrino, J. Suárez, S.A. Martí, M.A. 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. SER info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, F.
Bikiel, D.E.
Pellegrino, J.
Suárez, S.A.
Martí, M.A.
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.
format SER
author Doctorovich, F.
Bikiel, D.E.
Pellegrino, J.
Suárez, S.A.
Martí, M.A.
author_facet Doctorovich, F.
Bikiel, D.E.
Pellegrino, J.
Suárez, S.A.
Martí, M.A.
author_sort Doctorovich, F.
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
url http://hdl.handle.net/20.500.12110/paper_08988838_v64_n_p97_Doctorovich
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