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- W2170216400 abstract "Desulfotomaculum reducens MI-1 is a Firmicute strain capable of reducing a variety of heavy metal ions and has a great potential in heavy metal bioremediation. We recently identified Dred_2421 as a potential iron reductase through proteomic study of D. reducens. The current study examines its iron-reduction mechanism. Dred_2421, like its close homolog from Escherichia coli (2, 4-dienoyl-CoA reductase), has an FMN-binding N-terminal domain (NTD), an FAD-binding C-terminal domain (CTD), and a 4Fe–4S cluster between the two domains. To understand the mechanism of the iron-reduction activity and the role of each domain, we generated a series of variants for each domain and investigated their iron-reduction activity. Our results suggest that CTD is the main contributor of the iron-reduction activity, and that NTD and the 4Fe–4S cluster are not directly involved in such activity. This study provides a mechanistic understanding of the iron–reductase activity of Dred_2421 and may also help to elucidate other physiological activities this enzyme may have." @default.
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- W2170216400 date "2015-11-01" @default.
- W2170216400 modified "2023-09-25" @default.
- W2170216400 title "Molecular dissection of a putative iron reductase from Desulfotomaculum reducens MI-1" @default.
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- W2170216400 doi "https://doi.org/10.1016/j.bbrc.2015.10.016" @default.
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