Mechanism of Sulfide Binding by Ferric Hemeproteins
The reaction of hydrogen sulfide (H2S) with hemeproteins is a key physiological reaction; still, its mechanism and implications are not completely understood. In this work, we propose a combination of experimental and theoretical tools to shed light on the reaction in model system microperoxidase 11...
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American Chemical Society
2018
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| LEADER | 20159caa a22014417a 4500 | ||
|---|---|---|---|
| 001 | PAPER-25152 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205709.0 | ||
| 008 | 190410s2018 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-85049403471 | |
| 024 | 7 | |2 cas |a sulfide, 18496-25-8; Hemeproteins; Sulfides | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a INOCA | ||
| 100 | 1 | |a Boubeta, F.M. | |
| 245 | 1 | 0 | |a Mechanism of Sulfide Binding by Ferric Hemeproteins |
| 260 | |b American Chemical Society |c 2018 | ||
| 270 | 1 | 0 | |m Bari, S.E.; Instituto de Química Física de Los Materiales, Medio Ambiente y Energía, CONICET, Universidad de Buenos AiresArgentina; email: bari@qi.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The reaction of hydrogen sulfide (H2S) with hemeproteins is a key physiological reaction; still, its mechanism and implications are not completely understood. In this work, we propose a combination of experimental and theoretical tools to shed light on the reaction in model system microperoxidase 11 (MP11-FeIII) and myoglobin (Mb-FeIII), from the estimation of the intrinsic binding constants of the species H2S and hydrosulfide (HS-), and the computational description of the overall binding process. Our results show that H2S and HS- are the main reactive species in Mb-FeIII and MP11-FeIII, respectively, and that the magnitude of their intrinsic binding constants are similar to most of the binding constants reported so far for hemeproteins systems and model compounds. However, while the binding of HS- to Mb-FeIII was negligible, the binding of H2S to MP11-FeIII was significant, providing a frame for a discriminated analysis of both species and revealing differential mechanistic aspects. A joint inspection of the kinetic data and the free energy profiles of the binding processes suggests that a dissociative mechanism with the release of a coordinated water molecule as rate limiting step is operative in the binding of H2S to Mb-FeIII and that the binding of HS- is prevented in the access to the protein matrix. For the MP11-FeIII case, where no access restrictions for the ligands are present, an associative component in the mechanism seems to be operative. Overall, the results suggest that if accessing the active site then both H2S and HS- are capable of binding a ferric heme moiety. Copyright © 2018 American Chemical Society. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires, UBACYT 20020130100097BA | ||
| 536 | |a Detalles de la financiación: PICT 2015−2761 | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, 11220150100394CO, 11220150100303CO | ||
| 536 | |a Detalles de la financiación: #F.M.B. and S.A.B. contributed equally to this work. Funding This research was supported by grants of the Universidad de Buenos Aires, UBACYT 20020130100097BA and Agencia Nacional de Promocioń Cientıfí ca y Tecnologica,́ PICT 2014− 1022, PICT 2015−2761, and CONICET grants 11220150100303CO and 11220150100394CO. Notes The authors declare no competing financial interest. | ||
| 593 | |a Instituto de Química Física de Los Materiales, Medio Ambiente y Energía, CONICET, Universidad de Buenos Aires, Buenos Aires, 1053, Argentina | ||
| 593 | |a Departamento de Química Inorgánica, Analítica y Química Física, Universidad de Buenos Aires, Buenos Aires, 1053, Argentina | ||
| 593 | |a Instituto de Cálculo, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, 1053, Argentina | ||
| 690 | 1 | 0 | |a HEMOPROTEIN |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a SULFIDE |
| 690 | 1 | 0 | |a CHEMISTRY |
| 690 | 1 | 0 | |a METABOLISM |
| 690 | 1 | 0 | |a MOLECULAR MODEL |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a HEMEPROTEINS |
| 690 | 1 | 0 | |a HYDROGEN-ION CONCENTRATION |
| 690 | 1 | 0 | |a MODELS, MOLECULAR |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a SULFIDES |
| 650 | 1 | 7 | |2 spines |a PH |
| 700 | 1 | |a Bieza, S.A. | |
| 700 | 1 | |a Bringas, M. | |
| 700 | 1 | |a Estrin, D.A. | |
| 700 | 1 | |a Boechi, L. | |
| 700 | 1 | |a Bari, S.E. | |
| 773 | 0 | |d American Chemical Society, 2018 |g v. 57 |h pp. 7591-7600 |k n. 13 |p Inorg. Chem. |x 00201669 |w (AR-BaUEN)CENRE-60 |t Inorganic Chemistry | |
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