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Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments

Autor: S. Della Longa, Martin Weik, Thierry Prangé, Nathalie Colloc'h, Linda Celeste Montemiglio, Philippe Carpentier, C. Savino, Alessandro Arcovito, Cécile Exertier, Chiara Ardiccioni, Beatrice Vallone, Maurizio Brunori, P. van der Linden, G. Avella, Dominique Bourgeois

Publikováno v: International Union of Crystallography journal
International Union of Crystallography journal, International Union of Crystallography 2019, 5, 6 (5), pp.832-842. ⟨10.1107/S2052252519008157⟩
International Union of Crystallography journal, 2019, 6, pp.832-842. ⟨10.1107/S2052252519008157⟩
IUCrJ 6 (2019): 832–842. doi:10.1107/S2052252519008157
info:cnr-pdr/source/autori:Ardiccioni, Chiara; Arcovito, Alessandro; Della Longa, Stefano; van der Linden, Peter; Bourgeois, Dominique; Weik, Martin; Montemiglio, Linda Celeste; Savino, Carmelinda; Avella, Giovanna; Exertier, Cecile; Carpentier, Philippe; Prange, Thierry; Brunori, Maurizio; Colloc'h, Nathalie; Vallone, Beatrice/titolo:Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments/doi:10.1107%2FS2052252519008157/rivista:IUCrJ/anno:2019/pagina_da:832/pagina_a:842/intervallo_pagine:832–842/volume:6
IUCrJ, Vol 6, Iss 5, Pp 832-842 (2019)
IUCrJ
'IUCrJ ', vol: 6, pages: 832-842 (2019)

Ultralow-temperature X-ray crystallography, in crystallo microspectroscopy and X-ray absorption spectroscopy were used to study the carbon monoxide photodissociation intermediate in neuroglobin. Moreover, X-ray crystallography under high O2 pressure

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c081acfeba087904f76c199cad0b0e2
https://hal.archives-ouvertes.fr/hal-02270778

Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF

Autor: Oleksander Minkow, Maurizio Brunori, Karin Nienhaus, Alessandro Arcovito, Federica Draghi, Ulrich Nienhaus, Don C. Lamb

Publikováno v: Biophysical Chemistry. 109:41-58

Recombination of carbon monoxide to myoglobin mutants YQR and YQRF was studied using transient infrared absorption spectroscopy and Fourier transform infrared-temperature derivative spectroscopy (FTIR-TDS). Photoproduct states B, C', C" and D associa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63b4da666f0b18fae7c05981bd336f05
https://doi.org/10.1016/j.bpc.2003.10.002

Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography

Autor: Dominique Bourgeois, Friedrich Schotte, Alessandro Arcovito, Giuliano Sciara, Philip A. Anfinrud, Maurizio Brunori, Beatrice Vallone

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, 103 (13), pp.4924-4929. ⟨10.1073/pnas.0508880103⟩
Proceedings of the National Academy of Sciences of the United States of America, 2006, 103 (13), pp.4924-4929. ⟨10.1073/pnas.0508880103⟩

Work carried out over the last 30 years unveiled the role of structural dynamics in controlling protein function. Cavity networks modulate structural dynamics trajectories and are functionally relevant; in globins they have been assigned a role in li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c189945472b24b4554525c697b51e178
https://hal.archives-ouvertes.fr/hal-01617679

Proton linkage for CO binding and redox properties of bovine lactoperoxidase

Autor: Stefano Marini, Giampiero De Sanctis, Alessandro Arcovito, Roberto Santucci, Pia Ferrari Rosa, Andrea Bellelli, Chiara Ciaccio, Federica Sinibaldi, Elena Maria Ghibaudi, Massimo Coletta

Publikováno v: Biophysical journal
86 (2004): 448–454.
info:cnr-pdr/source/autori:Ciaccio C, De Sanctis G, Marini S, Sinibaldi F, Santucci R, Arcovito A, Bellelli A, Ghibaudi E, Ferrari Rosa P, Coletta M./titolo:Proton linkage for CO binding and redox properties of bovine lactoperoxidase./doi:/rivista:Biophysical journal (Print)/anno:2004/pagina_da:448/pagina_a:454/intervallo_pagine:448–454/volume:86
Scopus-Elsevier

The pH-dependence of redox properties and of CO binding to bovine lactoperoxidase has been investigated over the range between 2 and 11. The pH-dependence of redox potentials shows a biphasic behavior, suggesting the existence of (at least) two redox

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48da691bc0bd07e024a6461955217a59
http://hdl.handle.net/11573/105634