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• W2022863863 abstract "The transcription factor FNR ( f umarate n itrate r eduction) requires the presence of an iron-sulfur (Fe-S) cluster for its function as a global transcription regulator in Escherichia coli when oxygen becomes scarce. To define the oxidation state and type of Fe-S cluster present in the active form of FNR, we have studied anaerobically purified FNR with Mössbauer spectroscopy. Our data showed that this form of FNR contained a [4Fe-4S] 2+ cluster (δ = 0.45 mm/s; Δ E Q = 1.22 mm/s) and that the [4Fe-4S] 2+ cluster was rapidly destroyed on exposure of FNR to air. Under these conditions, the yellow–green active form of FNR turned deep red; analysis of sulfide indicated that 70% of the labile sulfide was still present, suggesting that the Fe-S cluster had been converted into a different form. Little [3Fe-4S] cluster was, however, detected by EPR. According to Mössbauer spectroscopy, the [4Fe-4S] 2+ cluster was converted in about 60% yield to a [2Fe-2S] 2+ cluster (δ = 0.28 mm/s; Δ E Q = 0.58 mm/s) following 17 min of exposure to air. The [2Fe-2S] 2+ cluster form of FNR was much more stable to oxygen, but was unable to sustain biological activity (e.g., DNA binding). However, DNA binding and the absorption spectrum characteristic of the [4Fe-4S] 2+ cluster could be largely restored from the [2Fe-2S] 2+ form when Cys, Fe, DTT, and the NifS protein were added. It has yet to be determined whether the form of FNR containing the [2Fe-2S] 2+ cluster has any biological significance, e.g., as an in vivo intermediate that is more rapidly converted to the active form than the apoprotein." @default.
• W2022863863 created "2016-06-24" @default.
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• W2022863863 date "1997-06-10" @default.
• W2022863863 modified "2023-10-03" @default.
• W2022863863 title "Iron-sulfur cluster disassembly in the FNR protein of <i>Escherichia coli</i> by O ₂ : [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity" @default.
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• W2022863863 doi "https://doi.org/10.1073/pnas.94.12.6087" @default.
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