scholarly journals Combined Biochemical, Biophysical, and Cellular Methods to Study Fe–S Cluster Transfer and Cytosolic Aconitase Repair by MitoNEET

Author(s):  
Cécile Mons ◽  
Ioana Ferecatu ◽  
Sylvie Riquier ◽  
Ewen Lescop ◽  
Cécile Bouton ◽  
...  
Keyword(s):  
2021 ◽  
Vol 51 (3) ◽  
pp. 780-787
Author(s):  
Sh. Hamada ◽  
Nourhan M. Elmedalaa ◽  
I. Bondouk ◽  
N. Darwish ◽  
Awad A. Ibraheem

1995 ◽  
Vol 73 (1-2) ◽  
pp. 74-84 ◽  
Author(s):  
D. Baddou ◽  
C. Rioux ◽  
R. J. Slobodrian ◽  
J. M. Nelson

Angular distributions of the differential cross sections and analysing powers were measured at an energy of 4.6 MeV. The results are compared with the distorted wave Born approximation predictions for two-nucleon transfer and for a deuteron-cluster transfer. The agreement is qualitative at best, and a discussion of alternatives to improve it is presented.


2012 ◽  
Vol 287 (15) ◽  
pp. 11649-11655 ◽  
Author(s):  
John A. Zuris ◽  
Syed S. Ali ◽  
Howard Yeh ◽  
Tung A. Nguyen ◽  
Rachel Nechushtai ◽  
...  

MitoNEET (mNT) is the founding member of the recently discovered CDGSH family of [2Fe-2S] proteins capable of [2Fe-2S] cluster transfer to apo-acceptor proteins. It is a target of the thiazolidinedione (TZD) class of anti-diabetes drugs whose binding modulate both electron transfer and cluster transfer properties. The [2Fe-2S] cluster in mNT is destabilized upon binding of NADPH, which leads to loss of the [2Fe-2S] cluster to the solution environment. Because mNT is capable of transferring [2Fe-2S] clusters to apo-acceptor proteins, we sought to determine whether NADPH binding also affects cluster transfer. We show that NADPH inhibits transfer of the [2Fe-2S] cluster to an apo-acceptor protein with an inhibition constant (Ki) of 200 μm, which reflects that of NADPH concentrations expected under physiological conditions. In addition, we determined that the strictly conserved cluster interacting residue Asp-84 in the CDGSH domain is necessary for the NADPH-dependent inhibition of [2Fe-2S] cluster transfer. The most critical cellular function of NADPH is in the maintenance of a pool of reducing equivalents, which is essential to counteract oxidative damage. Taken together, our findings suggest that NADPH can regulate both mNT [2Fe-2S] cluster levels in the cell as well as the ability of the protein to transfer [2Fe-2S] clusters to cytosolic or mitochondrial acceptors.


1970 ◽  
Vol 29 (2-3) ◽  
pp. 143-158 ◽  
Author(s):  
M. El-Nadi ◽  
A. Osman ◽  
T. H. Rihan

2014 ◽  
Vol 111 (17) ◽  
pp. 6203-6208 ◽  
Author(s):  
L. Banci ◽  
D. Brancaccio ◽  
S. Ciofi-Baffoni ◽  
R. Del Conte ◽  
R. Gadepalli ◽  
...  

FEBS Letters ◽  
2016 ◽  
Vol 590 (24) ◽  
pp. 4531-4540 ◽  
Author(s):  
Christine Wachnowsky ◽  
Insiya Fidai ◽  
James A. Cowan

2006 ◽  
Vol 765 (3-4) ◽  
pp. 277-293 ◽  
Author(s):  
A. Mitra ◽  
D.R. Chakrabarty ◽  
V.M. Datar ◽  
Suresh Kumar ◽  
E.T. Mirgule ◽  
...  

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