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中国生物工程杂志

China Biotechnology
China Biotechnology  2015, Vol. 35 Issue (10): 32-38    DOI: 10.13523/j.cb.20151005
    
Ferrichrome Binding Characteristics of Wild Type-and Mutant FtsBs in Streptococcus pyogenes
LI Hui1,2, XUE Wei1, SUN Xue-song2
1. Department of Biomedical Engineering Jinan University, Guanzhou 510632, China;
2. Institute of Life and Health Engineering, Jinan University, Guangzhou 510632, China
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Abstract  

Objective: To further compare the ferrichrome binding characteristics between wild type FtsB and mutant Y137A, W204A in Streptococcus pyogenes, and to further determine the ferrichrome binding sites. Methods: Wild type FtsB and Y137A, W204A mutant proteins were prepared. Their ferrichrome binding capacities were compared by ICP-MS and ITC; Their ferrichrome reduction rates were measured by UV-vis spectrometer using Na2S2O4 as the reductive agent; Their ferrichrome binding stabilities were analyzed via thermal and GuHCl denaturation. Results: The binding affinity and stability of the mutants Y137A and W204A with ferrichrome were both lower than that of wild-type FtsB. Whereas their ferrichrome reduction rates were higher than wild-type FtsB. Thus the residues Try137 and Trp204 play an important role in ferrichrome binding of FtsB. Conclutions: A valuable information for the understanding of ferrichrome transport in bacteria was provided, which may be helpful for the development of novel strategies in the control of bacterial infection.



Key wordsFtsB Mutant-proteins      Streptococcus pyogenes      Ferrichrome binding     
Received: 04 May 2015      Published: 25 October 2015
ZTFLH:  Q819  
Cite this article:

LI Hui, XUE Wei, SUN Xue-song. Ferrichrome Binding Characteristics of Wild Type-and Mutant FtsBs in Streptococcus pyogenes. China Biotechnology, 2015, 35(10): 32-38.

URL:

https://manu60.magtech.com.cn/biotech/10.13523/j.cb.20151005     OR     https://manu60.magtech.com.cn/biotech/Y2015/V35/I10/32

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