Molecular dissection of a putative iron reductase from Desulfotomaculum reducens MI-1 Academic Article uri icon

Overview

MeSH Major

  • Desulfotomaculum
  • FMN Reductase

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.┬áreducens. 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.

publication date

  • November 20, 2015

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC4649440

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2015.10.016

PubMed ID

  • 26454174

Additional Document Info

start page

  • 503

end page

  • 8

volume

  • 467

number

  • 3