Article ; Online: The H
2018 Volume 57, Issue 38, Page(s) 5616–5628
Abstract: Human mitoNEET (mNT) is the first identified Fe-S protein of the mammalian outer mitochondrial membrane. Recently, we demonstrated the involvement of mNT in a specific cytosolic pathway dedicated to the reactivation of oxidatively damaged cytosolic ... ...
Abstract | Human mitoNEET (mNT) is the first identified Fe-S protein of the mammalian outer mitochondrial membrane. Recently, we demonstrated the involvement of mNT in a specific cytosolic pathway dedicated to the reactivation of oxidatively damaged cytosolic aconitase by cluster transfer. In vitro studies using apo-ferredoxin (FDX) reveal that mNT uses an Fe-based redox switch mechanism to regulate the transfer of its cluster. Using the "gold standard" cluster recipient protein, FDX, we show that this transfer is direct and that only one of the two mNT clusters is transferred when the second one is decomposed. Combining complementary biophysical and biochemical approaches, we show that pH affects both the sensitivity of the cluster to O |
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MeSH term(s) | Ferredoxins/chemistry ; Ferredoxins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Hydrogen-Ion Concentration ; Iron/metabolism ; Iron-Sulfur Proteins/chemistry ; Iron-Sulfur Proteins/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Oxidation-Reduction ; Protein Multimerization ; Sulfur/metabolism |
Chemical Substances | CISD1 protein, human ; Ferredoxins ; Iron-Sulfur Proteins ; Mitochondrial Proteins ; apoferredoxin ; Sulfur (70FD1KFU70) ; Hydrogen Peroxide (BBX060AN9V) ; Iron (E1UOL152H7) |
Language | English |
Publishing date | 2018-09-11 |
Publishing country | United States |
Document type | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 1108-3 |
ISSN | 1520-4995 ; 0006-2960 |
ISSN (online) | 1520-4995 |
ISSN | 0006-2960 |
DOI | 10.1021/acs.biochem.8b00777 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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