Please use this identifier to cite or link to this item:
Title: Binding of the ferric uptake regulation repressor protein (Fur) to Mn(II), Fe(II), Co(II), and Cu(II) ions as co-repressors : electronic absorption, equilibrium, and 57Fe Mossbauer studies
Authors: Hamed, Mazen
Neilands, J. B.
Huynh, V.
Issue Date: May-1993
Publisher: ResearchGate
Abstract: The binding of the repressor protein (Fur) to Fe(H) as co-repressor was studied. Other transition metal ions such as M&I), Co(B), and Cu(I1) were also studied as models. From the equilibrium studies Kd values of 55,85,36, and 10 PM were obtained for the Fur complex with Fe(II), Mn(II), Co(II), and C&I), respectively. The ratio of metal to Fur monomer was 1:l in both the Fe(II) and M&I) complexes. Fur mutants were also studied. Electronic absorption spectra of the CofII) Fur complex gave evidence of a distorted tetrahedral Co(E) site bound to sulfur. Frozen solution 57Fe Miissbauer spectra of the Fe(B) Fur indicated the presence of Fe(II) in a high spin distorted octahedral environment. The role of the metal ion as co-repressor in the binding of Fur to DNA is discussed in view of the above results.
Description: Article published in : Journal of Inorganic Biochemistry. 1993 May 15;50(3):193-210
Appears in Collections:Fulltext Publications

Files in This Item:
File Description SizeFormat
Binding of the ferric uptake regulation repressor protein.pdf1.09 MBAdobe PDFView/Open
Show full item record

Page view(s)

Last Week
Last month
checked on Jun 27, 2024


checked on Jun 27, 2024

Google ScholarTM


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.