Reactivity of inorganic sulfide species toward a heme protein model

The reactivity of inorganic sulfide species toward heme peptides was explored under biorelevant conditions in order to unravel the molecular details of the reactivity of the endogenous hydrogen sulfide toward heme proteins. Unlike ferric porphyrinates, which are reduced by inorganic sulfide, some he...

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Autores principales:	Boubeta, Fernando Martin, Estrin, Dario Ariel, Boechi, Leonardo, Bari, Sara Elizabeth
Publicado:	2015
Materias:	hemoprotein hydrogen sulfide oligopeptide peroxidase protein binding sodium sulfide sulfide chemistry metabolism molecular dynamics protein conformation Hemeproteins Hydrogen Sulfide Molecular Dynamics Simulation Oligopeptides Peroxidases Protein Binding Protein Conformation Sulfides
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v54_n2_p527_Bieza http://hdl.handle.net/20.500.12110/paper_00201669_v54_n2_p527_Bieza
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00201669_v54_n2_p527_Bieza
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spelling	paper:paper_00201669_v54_n2_p527_Bieza2023-06-08T14:40:43Z Reactivity of inorganic sulfide species toward a heme protein model Boubeta, Fernando Martin Estrin, Dario Ariel Boechi, Leonardo Bari, Sara Elizabeth hemoprotein hydrogen sulfide oligopeptide peroxidase protein binding sodium sulfide sulfide chemistry metabolism molecular dynamics protein conformation Hemeproteins Hydrogen Sulfide Molecular Dynamics Simulation Oligopeptides Peroxidases Protein Binding Protein Conformation Sulfides The reactivity of inorganic sulfide species toward heme peptides was explored under biorelevant conditions in order to unravel the molecular details of the reactivity of the endogenous hydrogen sulfide toward heme proteins. Unlike ferric porphyrinates, which are reduced by inorganic sulfide, some heme proteins can form stable FeIII-sulfide adducts. To isolate the protein factors ruling the redox chemistry, we used as a system model, the undecapeptide microperoxidase (MP11), a heme peptide derived from cytochrome c proteolysis that retains the proximal histidine bound to the FeIII atom. Upon addition of gaseous hydrogen sulfide (H<inf>2</inf>S) at pH 6.8, the UV-vis spectra of MP11 closely resembled those of the low-spin ferric hydroxo complex (only attained at an alkaline pH) and cysteine or alkylthiol derivatives, suggesting that the FeIII reduction was prevented. The low-frequency region of the resonance Raman spectrum revealed the presence of an FeIII-S band at 366 cm-1 and the general features of a low-spin hexacoordinated heme. Anhydrous sodium sulfide (Na<inf>2</inf>S) was the source of sulfide of choice for the kinetic evaluation of the process. Theoretical calculations showed no distal stabilization mechanisms for bound sulfide species in MP11, highlighting a key role of the proximal histidine for the stabilization of the FeIII-S adducts of heme compounds devoid of distal counterparts, which is significant with regard to the biochemical reactivity of endogenous hydrogen sulfide. © 2014 American Chemical Society. Fil:Boubeta, F. 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. Fil:Boechi, L. 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. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v54_n2_p527_Bieza http://hdl.handle.net/20.500.12110/paper_00201669_v54_n2_p527_Bieza
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	hemoprotein hydrogen sulfide oligopeptide peroxidase protein binding sodium sulfide sulfide chemistry metabolism molecular dynamics protein conformation Hemeproteins Hydrogen Sulfide Molecular Dynamics Simulation Oligopeptides Peroxidases Protein Binding Protein Conformation Sulfides
spellingShingle	hemoprotein hydrogen sulfide oligopeptide peroxidase protein binding sodium sulfide sulfide chemistry metabolism molecular dynamics protein conformation Hemeproteins Hydrogen Sulfide Molecular Dynamics Simulation Oligopeptides Peroxidases Protein Binding Protein Conformation Sulfides Boubeta, Fernando Martin Estrin, Dario Ariel Boechi, Leonardo Bari, Sara Elizabeth Reactivity of inorganic sulfide species toward a heme protein model
topic_facet	hemoprotein hydrogen sulfide oligopeptide peroxidase protein binding sodium sulfide sulfide chemistry metabolism molecular dynamics protein conformation Hemeproteins Hydrogen Sulfide Molecular Dynamics Simulation Oligopeptides Peroxidases Protein Binding Protein Conformation Sulfides
description	The reactivity of inorganic sulfide species toward heme peptides was explored under biorelevant conditions in order to unravel the molecular details of the reactivity of the endogenous hydrogen sulfide toward heme proteins. Unlike ferric porphyrinates, which are reduced by inorganic sulfide, some heme proteins can form stable FeIII-sulfide adducts. To isolate the protein factors ruling the redox chemistry, we used as a system model, the undecapeptide microperoxidase (MP11), a heme peptide derived from cytochrome c proteolysis that retains the proximal histidine bound to the FeIII atom. Upon addition of gaseous hydrogen sulfide (H<inf>2</inf>S) at pH 6.8, the UV-vis spectra of MP11 closely resembled those of the low-spin ferric hydroxo complex (only attained at an alkaline pH) and cysteine or alkylthiol derivatives, suggesting that the FeIII reduction was prevented. The low-frequency region of the resonance Raman spectrum revealed the presence of an FeIII-S band at 366 cm-1 and the general features of a low-spin hexacoordinated heme. Anhydrous sodium sulfide (Na<inf>2</inf>S) was the source of sulfide of choice for the kinetic evaluation of the process. Theoretical calculations showed no distal stabilization mechanisms for bound sulfide species in MP11, highlighting a key role of the proximal histidine for the stabilization of the FeIII-S adducts of heme compounds devoid of distal counterparts, which is significant with regard to the biochemical reactivity of endogenous hydrogen sulfide. © 2014 American Chemical Society.
author	Boubeta, Fernando Martin Estrin, Dario Ariel Boechi, Leonardo Bari, Sara Elizabeth
author_facet	Boubeta, Fernando Martin Estrin, Dario Ariel Boechi, Leonardo Bari, Sara Elizabeth
author_sort	Boubeta, Fernando Martin
title	Reactivity of inorganic sulfide species toward a heme protein model
title_short	Reactivity of inorganic sulfide species toward a heme protein model
title_full	Reactivity of inorganic sulfide species toward a heme protein model
title_fullStr	Reactivity of inorganic sulfide species toward a heme protein model
title_full_unstemmed	Reactivity of inorganic sulfide species toward a heme protein model
title_sort	reactivity of inorganic sulfide species toward a heme protein model
publishDate	2015
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v54_n2_p527_Bieza http://hdl.handle.net/20.500.12110/paper_00201669_v54_n2_p527_Bieza
work_keys_str_mv	AT boubetafernandomartin reactivityofinorganicsulfidespeciestowardahemeproteinmodel AT estrindarioariel reactivityofinorganicsulfidespeciestowardahemeproteinmodel AT boechileonardo reactivityofinorganicsulfidespeciestowardahemeproteinmodel AT barisaraelizabeth reactivityofinorganicsulfidespeciestowardahemeproteinmodel
_version_	1768542922863542272

Reactivity of inorganic sulfide species toward a heme protein model

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