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A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]‐hydrogenase cofactor biosynthesis
Author(s) -
Fujishiro Takashi,
Ermler Ulrich,
Shima Seigo
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.059
Subject(s) - biosynthesis , cofactor , chemistry , iron–sulfur cluster , biochemistry , chaperone (clinical) , hydrogenase , gene cluster , function (biology) , metalloprotein , enzyme , stereochemistry , gene , biology , genetics , medicine , pathology
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.