Abstract:
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 (H2S) 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 (Na2S) 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.
Registro:
Documento: |
Artículo
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Título: | Reactivity of inorganic sulfide species toward a heme protein model |
Autor: | Bieza, S.A.; Boubeta, F.; Feis, A.; Smulevich, G.; Estrin, D.A.; Boechi, L.; Bari, S.E. |
Filiación: | Departamento de Química Inorgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires Ciudad Universitaria, Buenos Aires, C1428EHA, Argentina Instituto de Cálculo, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires Ciudad Universitaria, Buenos Aires, C1428EHA, Argentina Dipartimento di Chimica Ugo Schiff, Universita di Firenze, Via della Lastruccia 3-13, Sesto Fiorentino, Firenze, 50019, Italy
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Palabras clave: | 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 |
Año: | 2015
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Volumen: | 54
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Número: | 2
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Página de inicio: | 527
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Página de fin: | 533
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DOI: |
http://dx.doi.org/10.1021/ic502294z |
Título revista: | Inorganic Chemistry
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Título revista abreviado: | Inorg. Chem.
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ISSN: | 00201669
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CODEN: | INOCA
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CAS: | hydrogen sulfide, 15035-72-0, 7783-06-4; peroxidase, 9003-99-0; sodium sulfide, 1313-82-2; sulfide, 18496-25-8; Hemeproteins; Hydrogen Sulfide; microperoxidase; Oligopeptides; Peroxidases; sodium sulfide; Sulfides
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00201669_v54_n2_p527_Bieza |
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Citas:
---------- APA ----------
Bieza, S.A., Boubeta, F., Feis, A., Smulevich, G., Estrin, D.A., Boechi, L. & Bari, S.E.
(2015)
. Reactivity of inorganic sulfide species toward a heme protein model. Inorganic Chemistry, 54(2), 527-533.
http://dx.doi.org/10.1021/ic502294z---------- CHICAGO ----------
Bieza, S.A., Boubeta, F., Feis, A., Smulevich, G., Estrin, D.A., Boechi, L., et al.
"Reactivity of inorganic sulfide species toward a heme protein model"
. Inorganic Chemistry 54, no. 2
(2015) : 527-533.
http://dx.doi.org/10.1021/ic502294z---------- MLA ----------
Bieza, S.A., Boubeta, F., Feis, A., Smulevich, G., Estrin, D.A., Boechi, L., et al.
"Reactivity of inorganic sulfide species toward a heme protein model"
. Inorganic Chemistry, vol. 54, no. 2, 2015, pp. 527-533.
http://dx.doi.org/10.1021/ic502294z---------- VANCOUVER ----------
Bieza, S.A., Boubeta, F., Feis, A., Smulevich, G., Estrin, D.A., Boechi, L., et al. Reactivity of inorganic sulfide species toward a heme protein model. Inorg. Chem. 2015;54(2):527-533.
http://dx.doi.org/10.1021/ic502294z