| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7753799 | Journal of Inorganic Biochemistry | 2018 | 8 Pages |
Abstract
Cluster exchange chemistry for human glutaredoxin 5 (GLRX5) reveals distinct behavior from bacterial homologs with chaperones inhibiting rather than promoting cluster transfer from the ironâsulfur cluster scaffold protein ISCU1, and controlling the directionality of transfer. Human ironâsulfur cluster carrier protein NFU1 is identified as the most likely donor to GLRX5.112
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Joshua A. Olive, J.A. Cowan,