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• W2170476506 abstract "TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mössbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction." @default.
• W2170476506 created "2016-06-24" @default.
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• W2170476506 date "2014-06-09" @default.
• W2170476506 modified "2023-10-09" @default.
• W2170476506 title "TtcA a new tRNA-thioltransferase with an Fe-S cluster" @default.
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• W2170476506 doi "https://doi.org/10.1093/nar/gku508" @default.
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