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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todo:paper_00201669_v54_n2_p527_Bieza2023-10-03T14:17:09Z Reactivity of inorganic sulfide species toward a heme protein model Bieza, S.A. Boubeta, F. Feis, A. Smulevich, G. Estrin, D.A. Boechi, L. Bari, S.E. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Bieza, S.A. Boubeta, F. Feis, A. Smulevich, G. Estrin, D.A. Boechi, L. Bari, S.E. 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. |
| format |
JOUR |
| author |
Bieza, S.A. Boubeta, F. Feis, A. Smulevich, G. Estrin, D.A. Boechi, L. Bari, S.E. |
| author_facet |
Bieza, S.A. Boubeta, F. Feis, A. Smulevich, G. Estrin, D.A. Boechi, L. Bari, S.E. |
| author_sort |
Bieza, S.A. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00201669_v54_n2_p527_Bieza |
| work_keys_str_mv |
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1782026060519440384 |