The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH₂ to oxygen or ubiquinone.

ABSTRACT: Increasing evidence suggests that mitoNEET, a target of the type II diabetes drug pioglitazone, is a key regulator of energy metabolism in mitochondria. MitoNEET is anchored to the mitochondrial outer membrane via its N-terminal α helix domain and hosts a redox-active [2Fe-2S] cluster in its C-terminal cytosolic region. The mechanism by which mitoNEET regulates energy metabolism in mitochondria, however, is not fully understood. Previous studies have shown that mitoNEET specifically interacts with the reduced flavin mononucleotide (FMNH₂) and that FMNH₂ can quickly reduce the mitoNEET [2Fe-2S] clusters. Here we report that the reduced mitoNEET [2Fe-2S] clusters can be readily oxidized by oxygen. In the presence of FMN, NADH, and flavin reductase, which reduces FMN to

SUBMITTER: Wang Y 

PROVIDER: S-EPMC5473213 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature