Evaluation of iron(III) N,N'-ethylenebis[(o-hydroxyphenyl)glycinate] as a model for the iron binding site in the transferrins. 2

1983 ◽  
Vol 22 (18) ◽  
pp. 2630-2634 ◽  
Author(s):  
Marianne G. Patch ◽  
Kenneth P. Simolo ◽  
Carl J. Carrano
Keyword(s):  
Binding Site ◽  
Iron Binding

Characterization of the iron binding site in human 5-lipoxygenase by EPR spectroscopy

1993 ◽  
Vol 51 (1-2) ◽  
pp. 177
Author(s):  
N.D. Chasteen ◽  
J.K. Grady ◽  
M.D. Percival ◽  
D. Riendeau
Keyword(s):  
Binding Site ◽  
Epr Spectroscopy ◽  
Iron Binding

scholarly journals Mutational analysis of the iron binding site of Saccharomyces cerevisiae ferroxidase Fet3. An in vivo study

FEBS Letters ◽  
2001 ◽  
Vol 508 (3) ◽  
pp. 475-478 ◽  
Author(s):  
Maria Carmela Bonaccorsi di Patti ◽  
Maria Paola Paronetto ◽  
Valeria Dolci ◽  
Maria Rosa Felice ◽  
Amalia Lania ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Site ◽  
Mutational Analysis ◽  
In Vivo Study ◽  
Iron Binding

scholarly journals Characterization of the Iron-binding Site in Mammalian Ferrochelatase by Kinetic and Mössbauer Methods

1995 ◽  
Vol 270 (44) ◽  
pp. 26352-26357 ◽  
Author(s):  
Ricardo Franco ◽  
José J. G. Moura ◽  
Isabel Moura ◽  
Steven G. Lloyd ◽  
Boi Hanh Huynh ◽  
...  
Keyword(s):  
Binding Site ◽  
Iron Binding

scholarly journals The structure of neuromelanin and its iron binding site studied by infrared spectroscopy

FEBS Letters ◽  
1999 ◽  
Vol 457 (1) ◽  
pp. 18-22 ◽  
Author(s):  
M.G. Bridelli ◽  
D. Tampellini ◽  
L. Zecca
Keyword(s):  
Infrared Spectroscopy ◽  
Binding Site ◽  
Iron Binding

scholarly journals Identification of the miaB Gene, Involved in Methylthiolation of Isopentenylated A37 Derivatives in the tRNA of Salmonella typhimurium andEscherichia coli

1999 ◽  
Vol 181 (23) ◽  
pp. 7256-7265 ◽  
Author(s):  
Birgitta Esberg ◽  
Hon-Chiu Eastwood Leung ◽  
Ho-Ching Tiffany Tsui ◽  
Glenn R. Björk ◽  
Malcolm E. Winkler
Keyword(s):  
Escherichia Coli ◽  
Salmonella Typhimurium ◽  
Binding Site ◽  
Binding Sites ◽  
Open Reading Frame ◽  
Iron Binding ◽  
Reading Frame ◽  
Conserved Motif ◽  
E Coli ◽  
Weak Similarity

ABSTRACT The tRNA of the miaB2508::Tn10dCm mutant of Salmonella typhimurium is deficient in the methylthio group of the modified nucleosideN 6-(4-hydroxyisopentenyl)-2-methylthioadenosine (ms2io6A37). By sequencing, we found that the Tn10dCm of this strain had been inserted into thef474 (yleA) open reading frame, which is located close to the nag locus in both S. typhimurium and Escherichia coli. By complementation of the miaB2508::Tn10dCm mutation with a minimal subcloned f474 fragment, we showed thatf474 could be identified as the miaB gene, which is transcribed in the counterclockwise direction on the bacterial chromosome. Transcriptional studies revealed two promoters upstream ofmiaB in E. coli and S. typhimurium. A Rho-independent terminator was identified downstream of themiaB gene, at which the majority (96%) of themiaB transcripts terminate in E. coli, showing that the miaB gene is part of a monocistronic operon. A highly conserved motif with three cysteine residues was present in MiaB. This motif resembles iron-binding sites in other proteins. Only a weak similarity to an AdoMet-binding site was found, favoring the idea that the MiaB protein is involved in the thiolation step and not in the methylating reaction of ms2i(o)6A37 formation.

scholarly journals The effect of salt and site-directed mutations on the iron(III)-binding site of human serum transferrin as probed by EPR spectroscopy

1995 ◽  
Vol 309 (2) ◽  
pp. 403-410 ◽  
Author(s):  
J K Grady ◽  
A B Mason ◽  
R C Woodworth ◽  
N D Chasteen
Keyword(s):  
Binding Site ◽  
Epr Spectroscopy ◽  
Structural Changes ◽  
Hinge Region ◽  
Iron Binding ◽  
Chloride Binding ◽  
Binding Studies ◽  
Directed Mutation ◽  
Binding Isotherms ◽  
Binding Cleft

The effects of site-directed mutation and salt on the iron(III)-binding site of the recombinant half-molecule of the N-terminal lobe (hTf/2N) of human transferrin was studied by EPR spectroscopy. Changes were observed in the EPR spectra of all variants investigated (D63S, D63C, G65R, K206Q, H207E, H249E, H249Q, K296E and K296Q) compared with that of the wild-type protein. The most pronounced changes in the metal site were caused by replacement of the coordinating residues, Asp-63 and His-249, and the non-coordinating residue Lys-296, which is located in the hinge region of the iron-binding cleft. The EPR spectral changes from replacement of other non-coordinating residues were more subtle, indicating small changes in Fe3+ coordination to the protein. The EPR spectrum of variant G65R suggests that it adopts two distinct conformations in solution, one in which the two domains forming the iron-binding cleft are closed and one in which they are open; in the latter instance Asp-63 is no longer coordinated to the Fe3+. Chloride-binding studies on hTf/2N, K206Q, H207E, K296Q and K296E showed similar binding isotherms, indicating that none of the hinge region residues replaced, i.e. Lys-206, His-207 or Lys-296, are the sites of chloride binding. The results show that the coordination environment of the Fe3+ is sensitive to structural changes from site-directed mutation of both remote and coordinated residues and also to chloride-binding and ionic strength effects.

Sign in / Sign up

Export Citation Format

Share Document