scholarly journals [2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron–Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin

2013 ◽  
Vol 135 (22) ◽  
pp. 8117-8120 ◽  
Author(s):  
Jin Hae Kim ◽  
Ronnie O. Frederick ◽  
Nichole M. Reinen ◽  
Andrew T. Troupis ◽  
John L. Markley
PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e21992 ◽  
Author(s):  
Clara Iannuzzi ◽  
Salvatore Adinolfi ◽  
Barry D. Howes ◽  
Ricardo Garcia-Serres ◽  
Martin Clémancey ◽  
...  

Gene ◽  
2016 ◽  
Vol 585 (1) ◽  
pp. 159-165 ◽  
Author(s):  
Zarna Rajeshkumar Pala ◽  
Vishal Saxena ◽  
Gagandeep Singh Saggu ◽  
Sushil Kumar Yadav ◽  
R.P. Pareek ◽  
...  

2013 ◽  
Vol 825 ◽  
pp. 198-201 ◽  
Author(s):  
Jian She Liu ◽  
Lin Qian ◽  
Chun Li Zheng

Iron-sulfur (Fe-S) proteins are ubiquitous and participate in multiple essential functions of life. However, little is currently known about the mechanisms of iron-sulfur biosynthesis and transfer in acidophilic microorganisms. In this study, the IscS, IscU and IscA proteins from Acidithiobacillus ferrooxidans were successfully expressed in Escherichia coli and purified by affinity chromatography. The IscS was a cysteine desulfurase which catalyzes desulfurization of L-cysteine and transfer sulfur for iron-sulfur cluster assembly. Purified IscU did not have an iron-sulfur cluster but could act as a scaffold protein to assemble the [2Fe-2S] cluster in vitro. The IscA was a [4Fe-4S] cluster binding protein, but it also acted as an iron binding protein. Further studies indicated that the iron sulfur clusters could be transferred from pre-assembled scaffold proteins to apo-form iron sulfur proteins, the reconstituted iron sulfur proteins could restore their physiological activities.


2014 ◽  
Vol 459 (3) ◽  
pp. 467-478 ◽  
Author(s):  
Jan Rybniker ◽  
Florence Pojer ◽  
Jan Marienhagen ◽  
Gaëlle S. Kolly ◽  
Jeffrey M. Chen ◽  
...  

IscS of Mycobacterium tuberculosis is an essential component of iron–sulfur cluster assembly conferring resistance to oxidative stress. The strongly altered surface structure and the extensive protein-interaction network identified in the present study mirrors adaptations made in response to a heavily depleted mycobacterial ISC operon.


Biochemistry ◽  
2009 ◽  
Vol 48 (26) ◽  
pp. 6062-6071 ◽  
Author(s):  
Jin Hae Kim ◽  
Anna K. Füzéry ◽  
Marco Tonelli ◽  
Dennis T. Ta ◽  
William M. Westler ◽  
...  

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