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The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron

Authors
  • Grāve, Kristīne1
  • Griese, Julia J.1, 2
  • Berggren, Gustav3
  • Bennett, Matthew D.1
  • Högbom, Martin1
  • 1 Stockholm University, Svante Arrhenius väg 16C, Stockholm, 10691, Sweden , Stockholm (Sweden)
  • 2 Uppsala University, BMC, Uppsala, 75124, Sweden , Uppsala (Sweden)
  • 3 Uppsala University, Lägerhyddsvägen 1, Uppsala, 75120, Sweden , Uppsala (Sweden)
Type
Published Article
Journal
JBIC Journal of Biological Inorganic Chemistry
Publisher
Springer-Verlag
Publication Date
Apr 15, 2020
Volume
25
Issue
4
Pages
571–582
Identifiers
DOI: 10.1007/s00775-020-01782-3
Source
Springer Nature
Keywords
License
Green

Abstract

AbstractCorrect protein metallation in the complex mixture of the cell is a prerequisite for metalloprotein function. While some metals, such as Cu, are commonly chaperoned, specificity towards metals earlier in the Irving–Williams series is achieved through other means, the determinants of which are poorly understood. The dimetal carboxylate family of proteins provides an intriguing example, as different proteins, while sharing a common fold and the same 4-carboxylate 2-histidine coordination sphere, are known to require either a Fe/Fe, Mn/Fe or Mn/Mn cofactor for function. We previously showed that the R2lox proteins from this family spontaneously assemble the heterodinuclear Mn/Fe cofactor. Here we show that the class Ib ribonucleotide reductase R2 protein from Bacillus anthracis spontaneously assembles a Mn/Mn cofactor in vitro, under both aerobic and anoxic conditions, when the metal-free protein is subjected to incubation with MnII and FeII in equal concentrations. This observation provides an example of a protein scaffold intrinsically predisposed to defy the Irving–Williams series and supports the assumption that the Mn/Mn cofactor is the biologically relevant cofactor in vivo. Substitution of a second coordination sphere residue changes the spontaneous metallation of the protein to predominantly form a heterodinuclear Mn/Fe cofactor under aerobic conditions and a Mn/Mn metal center under anoxic conditions. Together, the results describe the intrinsic metal specificity of class Ib RNR and provide insight into control mechanisms for protein metallation.Graphical Abstract

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