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• W3195632982 endingPage "774" @default.
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• W3195632982 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 FeIII 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-NHis and Fe-SCys 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]+ clusters of one of the NEET proteins (mNT) is localized on the His-bound iron ion, consistently with our previous spectroscopic studies. Kinetic measurements demonstrate that the mNT [2Fe-2S]+ is released only by an increase in temperature. Thus, the reduced state of human NEET proteins [2Fe-2S] cluster is kinetically inert. This previously unrecognized kinetic inertness of the reduced state, along with the reactivity of the oxidized state, is unique across all [2Fe-2S] proteins. Finally, using a coevolutionary analysis, along with molecular dynamics simulations, we provide insight on the observed allostery between the loop L2 and the cluster region. Specifically, we show that W75, R76, K78, K79, F82 and G85 in the latter region share similar allosteric characteristics in both redox states." @default.
• W3195632982 created "2021-08-30" @default.
• W3195632982 creator A5009513269 @default.
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• W3195632982 creator A5075414334 @default.
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• W3195632982 date "2021-08-28" @default.
• W3195632982 modified "2023-09-27" @default.
• W3195632982 title "The two redox states of the human NEET proteins’ [2Fe–2S] clusters" @default.
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• W3195632982 doi "https://doi.org/10.1007/s00775-021-01890-8" @default.
• W3195632982 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8463382" @default.
• W3195632982 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34453614" @default.
• W3195632982 hasPublicationYear "2021" @default.
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