2015
DOI: 10.1021/tx500377b
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Abstract: Iron in iron overload disease is present as non-transferrin-bound iron, consisting of iron, citrate, and albumin. We investigated the redox properties of iron citrate by electrochemistry, by the kinetics of its reaction with ascorbate, by ESR, and by analyzing the products of reactions of ascorbate with iron citrate complexes in the presence of H2O2 with 4-hydroxybenzoic acid as a reporter molecule for hydroxylation. We report -0.03 V < E°' > +0.01 V for the (Fe(3+)-cit/Fe(2+)-cit) couple. The first step in th… Show more

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Cited by 46 publications
(34 citation statements)
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“…It can be concluded that 2.77 pH and 0.337 V Eh correspond to FeH 2 L + which is a stable soluble compound; this can be corroborated with previous studies [17].…”
Section: Pourbaix Diagram Of Iron-citrate Systemsupporting
confidence: 89%
“…It can be concluded that 2.77 pH and 0.337 V Eh correspond to FeH 2 L + which is a stable soluble compound; this can be corroborated with previous studies [17].…”
Section: Pourbaix Diagram Of Iron-citrate Systemsupporting
confidence: 89%
“…In particular, the Fe‐promoted formation of hydroxyl radical from peroxide (the Fenton reaction) is a common example . These metal catalysts are regenerated through electron transfer from other reducing substances that are available in cells, such as ascorbate and NADH . Therefore, a catalytic cycle can be sustained for these metal catalysts which will continuously promote the formation of ROS and the irreversible inactivation of substrates.…”
Section: Design Of Substrate‐selective Catalytic Metallodrugsmentioning
confidence: 99%
“…7 In the human body typical examples of Fe(III) binding proteins are lactotransferrin, transferrin and ferritin oxidizing Fe(II) to Fe(III) upon binding, and low molecular weight compounds in the blood also bind Fe(III), with citric acid being the major representative. 8 Also, amino acids, ATP/AMP, inositol phosphates and 2,5-dihydroxybenzoic acid have been described to chelate Fe(III) but not Fe(II). 9 A different picture emerges in the cytosolic compartment of cells, in which about 1 mM of Fe(II) predominates the labile iron pool, with glutathione in cellular concentrations ranging from 0.5 to 10 mM 10,11 acting as a buffer 9 and thus serving as a means for the subsequent incorporation of Fe(II) into a wide range of iron-dependent enzymes and electron transfer proteins.…”
Section: Redox Chemistry Of Ironmentioning
confidence: 99%