Biochemical characterization of bacterial FeoBs: A perspective on nucleotide specificity

Minhye Shin, Jinsub Park, Yerin Jin, In Jung Kim, Shelley M. Payne, Kyoung Heon Kim

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Iron is an essential requirement for the survival and virulence of most bacteria. The bacterial ferrous iron transporter protein FeoB functions as a major reduced iron transporter in prokaryotes, but its biochemical mechanism has not been fully elucidated. In the present study, we compared enzymatic properties of the cytosolic portions of pathogenic bacterial FeoBs to elucidate each bacterial strain-specific characteristic of the Feo system. We show that bacterial FeoBs are classified into two distinct groups that possess either a sole GTPase or an NTPase with a substrate promiscuity. This difference in nucleotide preference alters cellular requirements for monovalent and divalent cations. While the hydrolytic activity of the GTP-dependent FeoBs was stimulated by potassium, the action of the NTP-dependent FeoBs was not significantly affected by the presence of monovalent cations. Mutation of Asn11, having a role in potassium-dependent GTP hydrolysis, changed nucleotide specificity of the NTP-dependent FeoB, resulting in loss of ATPase activity. Sequence analysis suggested a possible association of alanine in the G5 motif for the NTP-dependent activity in FeoBs. This demonstration of the distinct enzymatic properties of bacterial FeoBs provides important insights into mechanistic details of Feo iron transport processes, as well as offers a promising species-specific anti-virulence target.

Original languageEnglish
Article number108350
JournalArchives of Biochemistry and Biophysics
Publication statusPublished - 2020 May 30

Bibliographical note

Funding Information:
Facility support from the Institute of Biomedical and Food Safety at CJ Food Safety Hall, Korea University is acknowledged.

Funding Information:
This research was supported by the C1 Gas Refinery Program ( 2016M3D3A1A01913268 ) and the Basic Science Research Program ( 2019R1I1A1A01058125 ), both through the National Research Foundation of Korea funded by the Korean Government (MSIT) .

Publisher Copyright:
© 2020 Elsevier Inc.


  • ATPase
  • Feo
  • Ferrous iron transport
  • GTPase
  • Potassium

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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