Hemoglobin Binding and Catalytic Heme Extraction by IsdB Near Iron Transporter Domains

Biochemistry ◽  
2014 ◽  
Vol 53 (14) ◽  
pp. 2286-2294 ◽  
Author(s):  
Catherine F. M. Bowden ◽  
Meghan M. Verstraete ◽  
Lindsay D. Eltis ◽  
Michael E. P. Murphy
Keyword(s):  
Iron Transporter ◽  
Hemoglobin Binding

scholarly journals NMR experiments redefine the hemoglobin binding properties of bacterial NEAr‐iron Transporter domains

2019 ◽  
Vol 28 (8) ◽  
pp. 1513-1523 ◽  
Author(s):  
Ramsay Macdonald ◽  
Brendan J. Mahoney ◽  
Ken Ellis‐Guardiola ◽  
Anthony Maresso ◽  
Robert T. Clubb
Keyword(s):  
Binding Properties ◽  
Iron Transporter ◽  
Hemoglobin Binding

scholarly journals Corrigendum to “Expression of Duodenal Iron Transporter Proteins in Diabetic Patients with and without Iron Deficiency Anemia”

2018 ◽  
Vol 2018 ◽  
pp. 1-1
Author(s):  
Efrat Broide ◽  
Ram Reifen ◽  
Shay Matalon ◽  
Zipi Berkovich ◽  
Maya Moshe ◽  
...  
Keyword(s):  
Iron Deficiency ◽  
Iron Deficiency Anemia ◽  
Deficiency Anemia ◽  
Diabetic Patients ◽  
Transporter Proteins ◽  
Iron Transporter

scholarly journals Hemoglobin-binding site on haptoglobin probed by selective proteolysis.

1983 ◽  
Vol 258 (2) ◽  
pp. 1227-1234
Author(s):  
J W Lustbader ◽  
J P Arcoleo ◽  
S Birken ◽  
J Greer
Keyword(s):  
Binding Site ◽  
Hemoglobin Binding ◽  
Selective Proteolysis

scholarly journals Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease

2006 ◽  
Vol 103 (31) ◽  
pp. 11503-11508 ◽  
Author(s):  
S. X. Wang ◽  
K. C. Pandey ◽  
J. R. Somoza ◽  
P. S. Sijwali ◽  
T. Kortemme ◽  
...  
Keyword(s):  
Structural Basis ◽  
Hemoglobin Binding

Human DMT1 as the candidate duodenal iron transporter

2000 ◽  
Vol 118 (4) ◽  
pp. A661
Author(s):  
Mark Thomas Worthington ◽  
Lauren Browne ◽  
Roger Qi Luo
Keyword(s):  
Iron Transporter

scholarly journals A Novel Iron Transporter SPD_1590 in Streptococcus pneumoniae Contributing to Bacterial Virulence Properties

2018 ◽  
Vol 9 ◽  
Author(s):  
Xinyu Miao ◽  
Jiaojiao He ◽  
Liang Zhang ◽  
Xinlu Zhao ◽  
Ruiguang Ge ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Bacterial Virulence ◽  
Iron Transporter ◽  
Virulence Properties

Fast determination of haptoglobin phenotype and calculation of hemoglobin binding capacity using high pressure gel permeation chromatography

2000 ◽  
Vol 291 (1) ◽  
pp. 43-51 ◽  
Author(s):  
J Delanghe ◽  
K Allcock ◽  
M Langlois ◽  
L Claeys ◽  
M De Buyzere
Keyword(s):  
High Pressure ◽  
Binding Capacity ◽  
Gel Permeation Chromatography ◽  
Fast Determination ◽  
Haptoglobin Phenotype ◽  
Hemoglobin Binding ◽  
Gel Permeation

The gene frpB2 of Helicobacter pylori encodes an hemoglobin-binding protein involved in iron acquisition

BioMetals ◽  
2009 ◽  
Vol 22 (6) ◽  
pp. 889-894 ◽  
Author(s):  
Marco A. González-López ◽  
José J. Olivares-Trejo
Keyword(s):  
Helicobacter Pylori ◽  
Binding Protein ◽  
Iron Acquisition ◽  
Hemoglobin Binding

scholarly journals Infection with Mycobacterium aviumDifferentially Regulates the Expression of Iron Transport Protein mRNA in Murine Peritoneal Macrophages

2001 ◽  
Vol 69 (11) ◽  
pp. 6618-6624 ◽  
Author(s):  
Wangjian Zhong ◽  
William P. Lafuse ◽  
Bruce S. Zwilling
Keyword(s):  
Host Defense ◽  
Transferrin Receptor ◽  
Iron Transport ◽  
Peritoneal Macrophages ◽  
Natural Resistance ◽  
Intracellular Pathogens ◽  
Mrna Levels ◽  
Iron Availability ◽  
Iron Transporter ◽  
Murine Peritoneal Macrophages

ABSTRACT Iron is an important element for the growth of microorganisms as well as in the defense of the host by serving as a catalyst for the generation of free radicals via the Fenton/Haber-Weiss reactions. The iron transporter natural resistance-associated macrophage protein 1 (Nramp1) confers resistance to the growth of a variety of intracellular pathogens including Mycobacterium avium. Recently several other proteins that are involved in iron transport, including the highly homologous iron transporter Nramp2 and the transferrin receptor-associated protein HFE (hereditary hemochromatosis protein), have been described. The relationship of these proteins to host defense and to the growth of intracellular pathogens is not known. Here, we report that infection with M. avium differentially regulates mRNA expression of the proteins associated with iron transport in murine peritoneal macrophages. Both Nramp1 and Nramp2 mRNA levels increase following infection, while the expression of transferrin receptor mRNA decreases. The level of expression of HFE mRNA remains unchanged. The difference in the expression of the mRNA of these proteins following infection or cytokine stimulation suggests that they may play an important role in host defense by maintaining a delicate balance between iron availability for host defense and at the same time limiting iron availability for microbial growth.

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