Thermosynechoccus 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-Reference-Cited by-同舟云学术

Thermosynechoccus 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

Published:2010-01-20 Issue:4 Volume:277 Page:903-917
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Alaleona Flaminia,Franceschini Stefano,Ceci Pierpaolo,Ilari Andrea,Chiancone Emilia

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2009.07532.x/fullpdf

Reference41 articles.

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2. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps;Martinez;J Bacteriol,1997

3. Dps protects cells against multiple stresses during stationary phase;Nair;J Bacteriol,2004

4. DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus;Ceci;Nucleic Acids Res,2004

5. The N-terminal extensions of Deinococcus radiodurans Dps-1 mediate DNA major groove interactions as well as assembly of the dodecamer;Bhattacharyya;J Biol Chem,2007

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