| Autor: |
John A. Zuris, Rachel Nechushtai, Mark L. Paddock, Howard Yeh, Patricia A. Jennings, Tung A. Nguyen, Syed S. Ali |
| Rok vydání: |
2012 |
| Předmět: |
|
| Zdroj: |
Biophysical Journal. 102(3) |
| ISSN: |
0006-3495 |
| DOI: |
10.1016/j.bpj.2011.11.2518 |
| Popis: |
MitoNEET is the founding member of the recently discovered CDGSH family of [2Fe-2S] proteins. Its structure contains a unique homodimeric fold with each monomer containing one [2Fe-2S] cluster (1). MitoNEET is a target of the thiazolidinedione (TZD) class of anti-diabetes drugs (2). Recently, it was reported that the [2Fe-2S] cluster in mitoNEET is destabilized upon binding of NADPH/NADP+ (3). As mitoNEET is capable of transferring its [2Fe-2S] clusters to an apo-acceptor protein (4) and an obvious question to ask is whether NADPH binding accelerates or abrogates cluster transfer. We show that NADPH blocks transfer of mitoNEET's [2Fe-2S] cluster to an apo-acceptor protein (see Figure). This suggests a likely functional role for the mitoNEET:NADPH/NADP+ interaction.(1) Paddock ML et al. (2007) PNAS 104 14342-7(2) Colca JR et al. (2004) Am J Physiol Endocrinol Metab 286 E252-60(3) Zhou et al. (2010) Biochemistry 49 9604-12(4) Zuris JA et al. (2011) PNAS 108 13047-52∗Supported by the Heme and Blood Proteins Training Grant 5T32DK007233-34View Large Image | View Hi-Res Image | Download PowerPoint Slide |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
