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• W1914804546 endingPage "14010" @default.
• W1914804546 startingPage "14002" @default.
• W1914804546 abstract "Singlet oxygen ((1)O2) is an important reactive oxygen species in biology that has deleterious effects. Proteins constitute the main target of (1)O2 in cells. Several organisms are able to mount a transcriptional defense against (1)O2. ChrR and MBS are two proteins with Zn(Cys)2(His)2 zinc finger sites that are involved in the regulation of the defense against (1)O2. In this article, we investigate the reactivity of Zn⋅CPF, a Zn(Cys)2(His)2 classical ββα zinc finger, with (1)O2. We show that Zn⋅CPF interacts with (1)O2 mainly by physical quenching using a combination of (1)O2 luminescence quenching and kinetic competition experiments. The chemical reaction, which accounts for 5% of the interaction, leads to oxidation of cysteines but not histidines. Primary photooxidation products, identified by HPLC and mass spectrometry, are sulfinate (75±5%) and disulfides (25±5%). The peptides that have a single cysteine thiolate oxidized into a sulfinate are still able to bind one equivalent Zn(2+) but with a dramatic reduction of the binding constant compared to Zn⋅CPF despite the preservation of the ββα fold, as shown by NMR and CD titrations. Finally, Zn⋅CPF is compared to Zn⋅LTC, a treble clef Zn(Cys)4 zinc finger, to gain further insight into the behavior of zinc fingers toward (1)O2." @default.
• W1914804546 created "2016-06-24" @default.
• W1914804546 creator A5011452544 @default.
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• W1914804546 creator A5078168503 @default.
• W1914804546 creator A5088730507 @default.
• W1914804546 date "2015-08-13" @default.
• W1914804546 modified "2023-09-26" @default.
• W1914804546 title "Reactivity of a Zn(Cys)₂(His)₂Zinc Finger with Singlet Oxygen: Oxidation Directed toward Cysteines but not Histidines" @default.
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• W1914804546 doi "https://doi.org/10.1002/chem.201501749" @default.
• W1914804546 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26270157" @default.
• W1914804546 hasPublicationYear "2015" @default.
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