interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Autor: Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D

Publikováno v: Biochimica et biophysica acta
1840 (2013): 535–544.
info:cnr-pdr/source/autori:Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D/titolo:interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc./doi:/rivista:Biochimica et biophysica acta (Print)/anno:2013/pagina_da:535/pagina_a:544/intervallo_pagine:535–544/volume:1840

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::f0d2c0073ff87098a938eb1fa432cdec
http://www.cnr.it/prodotto/i/276606

Thermosynechococcus elongatus DpsA binds Zn(II) at a unique three histidine-containing ferroxidase center and utilizes O2 as iron oxidant with very high efficiency, unlike the typical Dps proteins

Autor: Alaleona F, Franceschini S, Ceci P, Ilari A, Chiancone E.

Publikováno v: The FEBS journal
277 (2010): 903–917. doi:10.1111/j.1742-4658.2009.07532.x
info:cnr-pdr/source/autori:Alaleona F, Franceschini S, Ceci P, Ilari A, Chiancone E./titolo:Thermosynechococcus elongatus DpsA binds Zn(II) at a unique three histidine-containing ferroxidase center and utilizes O2 as iron oxidant with very high efficiency, unlike the typical Dps proteins/doi:10.1111%2Fj.1742-4658.2009.07532.x/rivista:The FEBS journal (Print)/anno:2010/pagina_da:903/pagina_a:917/intervallo_pagine:903–917/volume:277

The cyanobacterium Thermosynechococcus elongatus is one the few bacteria to possess two Dps proteins, DpsA-Te and Dps-Te. The present characterization of DpsA-Te reveals unusual structural and functional features that differentiate it from Dps-Te and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::9c09e07787067697497486f3535c4954

An ancient bacterial zinc acquisition system identified from a cyanobacterial exoproteome.

Autor: Sarasa-Buisan, Cristina¹ (AUTHOR), Ochoa de Alda, Jesús A. G.² (AUTHOR), Velázquez-Suárez, Cristina³ (AUTHOR), Rubio, Miguel Ángel³ (AUTHOR), Gómez-Baena, Guadalupe⁴ (AUTHOR), Fillat, María F.¹ (AUTHOR) fillat@unizar.es, Luque, Ignacio³ (AUTHOR) fillat@unizar.es

Publikováno v: PLoS Biology. 3/11/2024, Vol. 22 Issue 3, p1-33. 33p.

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.

Autor: Ilari A; CNR Institute of Molecular Biology and Pathology and Department of Biochemical Sciences, 'Sapienza' University of Rome, Piazzale A. Moro 5, 00185 Rome, Italy., Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E

Publikováno v: Biochimica et biophysica acta [Biochim Biophys Acta] 2014 Jan; Vol. 1840 (1), pp. 535-44. Date of Electronic Publication: 2013 Oct 12.