scholarly journals Two Distinct Ferritin-like Molecules inPseudomonas aeruginosa: The Product of thebfrAGene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)

Biochemistry ◽  
2011 ◽  
Vol 50 (23) ◽  
pp. 5236-5248 ◽  
Author(s):  
Huili Yao ◽  
Grace Jepkorir ◽  
Scott Lovell ◽  
Pavithra V. Nama ◽  
Saroja Weeratunga ◽  
...  
Keyword(s):  
Bacterial Ferritin

scholarly journals Spectroscopic Evidence for and Characterization of a Trinuclear Ferroxidase Center in Bacterial Ferritin from Desulfovibrio vulgaris Hildenborough

2012 ◽  
Vol 134 (26) ◽  
pp. 10822-10832 ◽  
Author(s):  
Alice S. Pereira ◽  
Cristina G. Timóteo ◽  
Márcia Guilherme ◽  
Filipe Folgosa ◽  
Sunil G. Naik ◽  
...  
Keyword(s):  
Desulfovibrio Vulgaris ◽  
Spectroscopic Evidence ◽  
Ferroxidase Center ◽  
Bacterial Ferritin ◽  
Desulfovibrio Vulgaris Hildenborough

Spectroelectrochemical investigation of Azotobacter vinelandii bacterial ferritin

1998 ◽  
Vol 44 (2) ◽  
pp. 301-307 ◽  
Author(s):  
He-Qing Huang ◽  
Feng-Zhang Zhang ◽  
Liang-Shu Xu ◽  
Qing-Mei Lin ◽  
Jing-Wei Huang ◽  
...  
Keyword(s):  
Azotobacter Vinelandii ◽  
Bacterial Ferritin

Iron(2+) and phosphate interactions in bacterial ferritin from Azotobacter vinelandii

Biochemistry ◽  
1992 ◽  
Vol 31 (24) ◽  
pp. 5672-5679 ◽  
Author(s):  
Gerald D. Watt ◽  
Richard B. Frankel ◽  
Deloria Jacobs ◽  
Heqing Huang ◽  
Georgia C. Papaefthymiou
Keyword(s):  
Azotobacter Vinelandii ◽  
Bacterial Ferritin

Characterization of a non-haem ferritin of the Archaeon Halobacterium salinarum, homologous to Dps (starvation-induced DNA-binding protein)

2002 ◽  
Vol 30 (4) ◽  
pp. 713-715 ◽  
Author(s):  
S. Reindel ◽  
C. L. Schmidt ◽  
S. Anemüller ◽  
B. F. Matzanke
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Visible Spectrum ◽  
Dna Binding Protein ◽  
Halobacterium Salinarum ◽  
Bacterial Ferritin ◽  
Uv Visible ◽  
Pcc 7942 ◽  
Fe Ions

An iron-rich protein was isolated from the Archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC 7942. It consists of 20 kDa subunits, forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 103 Fe ions/mol of holoprotein. CD spectra are consistent with an α-helical contribution of 58%. The UV/visible spectrum provides no evidence for the presence of haem groups. This protein exhibits features of a non-haem-type bacterial ferritin although it shares only little sequence homology with non-haem bacterial ferritin.

On the mineral core of ferritin-like proteins: structural and magnetic characterization

Nanoscale ◽  
2016 ◽  
Vol 8 (2) ◽  
pp. 1088-1099 ◽  
Author(s):  
A. García-Prieto ◽  
J. Alonso ◽  
D. Muñoz ◽  
L. Marcano ◽  
A. Abad Díaz de Cerio ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pyrococcus Furiosus ◽  
Magnetic Study ◽  
Magnetic Characterization ◽  
Bacterial Ferritin ◽  
Horse Spleen Ferritin ◽  
Mineral Core

We report a combined structural and magnetic study of the mineral core biomineralized by horse spleen ferritin and three prokaryotic ferritin-like proteins: bacterial ferritin and bacterioferritin from Escherichia coli and archaeal ferritin from Pyrococcus furiosus.

scholarly journals Magnetic Resonance Imaging of Tumors Colonized with Bacterial Ferritin-Expressing Escherichia coli

PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e25409 ◽  
Author(s):  
Philip J. Hill ◽  
Jochen Stritzker ◽  
Miriam Scadeng ◽  
Ulrike Geissinger ◽  
Daniel Haddad ◽  
...  
Keyword(s):  
Magnetic Resonance Imaging ◽  
Escherichia Coli ◽  
Magnetic Resonance ◽  
Resonance Imaging ◽  
Bacterial Ferritin

scholarly journals Evidence for Mössbauer spectroscopy for different forms of iron core in Pseudomonas aeruginosa bacterial ferritin

1990 ◽  
Vol 272 (1) ◽  
pp. 263-264 ◽  
Author(s):  
N M K Reid ◽  
D P E Dickson ◽  
C Greenwood ◽  
A Thompson ◽  
F H A Kadir ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Mössbauer Spectroscopy ◽  
Mossbauer Spectroscopy ◽  
Growth Conditions ◽  
Spectroscopic Studies ◽  
Iron Core ◽  
Whole Cells ◽  
Predominant Form ◽  
Bacterial Ferritin ◽  
Forms Of Iron

Mössbauer spectroscopic studies of whole cells of Pseudomonas aeruginosa, grown under different conditions, indicate that the predominant form of iron in the cells varies significantly. These differences are interpreted in terms of differences in the nature of the iron cores of the bacterial ferritin, which result from different growth conditions.

scholarly journals Characterization of the DNA-Mediated Oxidation of Dps, A Bacterial Ferritin

2016 ◽  
Vol 138 (35) ◽  
pp. 11290-11298 ◽  
Author(s):  
Anna R. Arnold ◽  
Andy Zhou ◽  
Jacqueline K. Barton
Keyword(s):  
Bacterial Ferritin ◽  
Mediated Oxidation
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