Structural Characterization of Ferric Hemoglobins from Three Antarctic Fish Species of the Suborder Notothenioidei

Autor: Vergara, Alessandro, Franzese, Marisa, Merlino, Antonello, Vitagliano, Luigi, Verde, Cinzia, di Prisco, Guido, Caroline Lee, H., Peisach, Jack, Mazzarella, Lelio

Publikováno v: In Biophysical Journal 2007 93(8):2822-2829

Understanding the binding properties of an unusual metal-binding protein − a study of bacterial frataxin.

Autor: Pastore, Chiara¹, Franzese, Marisa², Sica, Filomena^2,3, Temussi, Pierandrea^1,2, Pastore, Annalisa¹ apastor@nimr.mrc.ac.uk

Publikováno v: FEBS Journal. Aug2007, Vol. 274 Issue 16, p4199-4210. 12p. 4 Diagrams, 1 Chart, 1 Graph.

Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins

Autor: Alessandro Vergara, Franzese, Marisa, Antonello Merlino, Bonomi, Giovanna, Verde, C., Giordano, D., Di Prisco, G., Lee, C., Peisach, J., Mazzarella, Lelio

Publikováno v: Università degli Studi di Napoli Federico II
37° Congresso Nazionale di Chimica Fisica, Camogli, 2008
info:cnr-pdr/source/autori:A. Vergara, M. Franzese, A. Merlino, G. Bonomi, C. Verde, D. Giordano, G. di Prisco, H. C. Lee, J. Peisach, L. Mazzarella/congresso_nome:37° Congresso Nazionale di Chimica Fisica/congresso_luogo:Camogli/congresso_data:2008/anno:2008/pagina_da:/pagina_a:/intervallo_pagine

Oxidation of hemoglobins leads to the formation of Fe(III) forms, whose relevance spans from biochemical to physiological aspects 1. Here we report a combined EPR/X-ray crystallography study at acidic pH on six ferric tetrameric hemoglobins (Hbs), fi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::58a08101cead498462b740dcf0ecd17b
http://hdl.handle.net/11588/346249

Linkage between Root effect and hemichrome stability

Autor: Alessandro Vergara, Antonello Merlino, Franzese, Marisa, Di Prisco, G., Verde, C., Peisach, J., Lee, C., Mazzarella, Lelio

Publikováno v: Università degli Studi di Napoli Federico II
VII European Symposium of the. Protein Society, Stoccolma, 2007
info:cnr-pdr/source/autori:A.Vergara, A. Merlino, M. Franzese, G. Di Prisco, C. Verde, J. Peisach, C. Lee, L. Mazzarella/congresso_nome:VII European Symposium of the. Protein Society/congresso_luogo:Stoccolma/congresso_data:2007/anno:2007/pagina_da:/pagina_a:/intervallo_pagine

Antarctic fish hemoglobins (AFHbs) exhibit a peculiar oxidation process. Upon oxidation, these tetrameric proteins show a remarkable propensity to evolve toward the formation of hemichrome, a species in which both proximal and distal hystidines are b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::324f486fa38682e6647b037e733bd15c
http://hdl.handle.net/11588/307836

Stereochemistry, formation and reactivity of hemichromes in Antarctic fish hemoglobins

Autor: Alessandro Vergara, Antonello Merlino, Franzese, Marisa, Di Prisco, G., Verde, C., Peisach, J., Lee, C., Mazzarella, Lelio

Publikováno v: XIVth International Conference on Dioxygen binding and sensing proteins, Napoli, 2006
info:cnr-pdr/source/autori:A.Vergara, A. Merlino, M. Franzese, G. Di Prisco, C. Verde, J. Peisach, C. Lee, L. Mazzarella/congresso_nome:XIVth International Conference on Dioxygen binding and sensing proteins/congresso_luogo:Napoli/congresso_data:2006/anno:2006/pagina_da:/pagina_a:/intervallo_pagine
Università degli Studi di Napoli Federico II

Antarctic fish hemoglobins (AF-Hbs) exhibit an unusual auto-oxidation process. Our previous crystallographic and spectroscopic investigations have demonstrated that, upon oxidation, these tetrameric proteins show a remarkable propensity to evolve tow

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3684618625f9bb256b47314ec450003c
http://hdl.handle.net/11588/307834