The two redox states of the human NEET proteins' [2Fe-2S] clusters.

ABSTRACT: The NEET proteins constitute a unique class of [2Fe-2S] proteins. The metal ions bind to three cysteines and one histidine. The proteins' clusters exist in two redox states; the oxidized protein (containing two Fe^III ions) can transfer the cluster to apo-acceptor protein(s), while the reduced form (containing one ferrous ion) remains bound to the protein frame. Here, we perform in silico and in vitro studies on human NEET proteins in both reduced and oxidized forms. Quantum chemical calculations on all available human NEET proteins structures suggest that reducing the cluster weakens the Fe-N^His and Fe-S^Cys bonds, similar to what is seen in other Fe-S proteins (e.g., ferredoxin and Rieske protein). We further show that the extra electron in the [2Fe-2S]

SUBMITTER: Zuo K 

PROVIDER: S-EPMC8463382 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature