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Honarmand Ebrahimi, Kourosh (author), Ciofi-Baffoni, Simone (author), Hagedoorn, P.L. (author), Nicolet, Yvain (author), Le Brun, Nick E. (author), Hagen, W.R. (author), Armstrong, Fraser A. (author)
A virus hijacks host cellular machineries and metabolites in order to reproduce. In response, the innate immune system activates different processes to fight back. Although many aspects of these processes have been well investigated, the key roles played by iron–sulfur [FeS] clusters, which are among the oldest classes of bio-inorganic...
review 2022
document
Hagen, W.R. (author), Hagedoorn, P.L. (author), Honarmand Ebrahimi, K. (author)
Biochemistry of the essential element iron is complicated by radical chemistry associated with Fe(II) ions and by the extremely low solubility of the Fe(III) ion in near-neutral water. To mitigate these problems cells from all domains of life synthesize the protein ferritin to take up and oxidize Fe(II) and to form a soluble storage of Fe(III)...
journal article 2017
document
van Schie, M.M.C.H. (author), Honarmand Ebrahimi, K. (author), Hagen, Wilfred R. (author), Hagedoorn, P.L. (author)
Recent developments in microfluidic and nanofluidic technologies have resulted in development of new chip-based microfluidic calorimeters with potential use in different fields. One application would be the accurate high-throughput measurement of enzyme activity. Calorimetry is a generic way to measure activity of enzymes, but unlike...
journal article 2017
document
Honarmand Ebrahimi, K. (author), Bill, Eckhard (author), Hagedoorn, P.L. (author), Hagen, W.R. (author)
Ferritin is a nanocage protein made of 24 subunits. Its major role is to manage intracellular concentrations of free Fe(ii) and Fe(iii) ions, which is pivotal for iron homeostasis across all domains of life. This function of the protein is regulated by a conserved di-iron catalytic center and has been the subject of extensive studies over the...
journal article 2016
document
Honarmand Ebrahimi, K. (author), Hagedoorn, P.L. (author), Hagen, W.R. (author)
journal article 2015
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Honarmand Ebrahimi, K. (author), Dienemann, C. (author), Hoefgens, S. (author), Than, M.E. (author), Hagedoorn, P.L. (author), Hagen, W.R. (author)
The ubiquitous 24-meric iron-storage protein ferritin and multicopper oxidases such as ceruloplasmin or hephaestin catalyze oxidation of Fe(II) to Fe(III), using molecular oxygen as oxidant. The ferroxidase activity of these proteins is essential for cellular iron homeostasis. It has been reported that the amyloid precursor protein (APP) also...
journal article 2013
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Honarmand Ebrahimi, K. (author), Hagedoorn, P.L. (author), Hagen, W.R. (author)
The ?-amyloid precursor protein (APP), which is a key player in Alzheimer's disease, was recently reported to possess an Fe(II) binding site within its E2 domain which exhibits ferroxidase activity [Duce et al. 2010, Cell 142: 857]. The putative ligands of this site were compared to those in the ferroxidase site of ferritin. The activity was...
journal article 2012
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Honarmand Ebrahimi, K. (author), Hagedoorn, P.L. (author), Van der Weel, L. (author), Verhaert, P.D.E.M. (author), Hagen, W.R. (author)
Storage of iron in a nontoxic and bioavailable form is essential for many forms of life. Three subfamilies of the ferritin-like superfamily, namely, ferritin, bacterioferritin, and Dps (DNA-binding proteins from starved cells), are able to store iron. Although the function of these iron-storage proteins is constitutive to many organisms to...
journal article 2012
document
Honarmand Ebrahimi, K. (author), Hagedoorn, P.L. (author), Hagen, W.R. (author)
Ferritin is a ubiquitous iron-storage protein that has 24 subunits. Each subunit of ferritins that exhibit high Fe(II) oxidation rates has a diiron binding site, the socalled ferroxidase center (FC). The role of the FC appears to be essential for the iron-oxidation catalysis of ferritins. Studies of the iron oxidation by mammalian, bacterial,...
journal article 2010
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