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  A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis

Fujishiro, T., Ermler, U., & Shima, S. (2014). A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis. FEBS Letters, 588(17), 2789-2793. doi:10.1016/j.febslet.2014.05.059.

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 Creators:
Fujishiro, T.1, Author           
Ermler, U., Author
Shima, S.1, Author           
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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Free keywords: Hydrogenase; Iron; Metal-cofactor biosynthesis; Metal-binding protein; X-ray crystallography; Nif3-like protein family
 Abstract: HcgD, a homolog of the ubiquitous Nif3-like protein family, is found in a gene cluster involved in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase. The presented crystal structure and biochemical analyses indicated that HcgD has a dinuclear iron-center, which provides a pronounced binding site for anionic ligands. HcgD contains a stronger and a weaker bound iron; the latter being removable by chelating reagents preferentially in the oxidized state. Therefore, we propose HcgD as an iron chaperone in FeGP cofactor biosynthesis, which might also stimulate investigations on the functionally unknown but physiologically important eukaryotic Nif3-like protein family members.

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Language(s): eng - English
 Dates: 2014-08-25
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 708734
ISI: 000340882900005
DOI: 10.1016/j.febslet.2014.05.059
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 588 (17) Sequence Number: - Start / End Page: 2789 - 2793 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501