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Glutathione: a key component of the cytoplasmic labile iron pool | BioMetals
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The cytoplasmic labile iron pool supplies iron to the mitochondrion for heme and iron sulfur cluster synthesis and to many cytoplasmic enzymes, thereby controlling numerous metabolic reactions. Surprisingly the chemical nature of this pool has never been convincingly characterised. Here we provide evidence for iron(II)glutathione being the dominant component of this pool. We report for the first time the affinity constant for the glutathioneāiron(II) interaction and use this value to study the cytoplasmic speciation of iron(II). The formation of this complex is a major determinant of the electrode potential of the cytoplasmic ferrous iron pool, a means of selecting between iron(II) and manganese(II) and it provides a substrate for glutaredoxin/iron clusters at the dimer interface of glutaredoxins involved in the synthesis of FeāS cluster proteins.
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google, scholar, article, cas, pubmed, iron, chem, glutathione, pool, biol, cytoplasmic, cluster, content, hider, access, metal, biochem, privacy, cookies, labile, kong, fes, soc, cell, complexes, publish, search, nature, ironii, glutaredoxins, proteins, regulatory, cells, blood, metabolism, cellular, sci, nat, function, data, information, log, journal, research, biometals, component, robert, heme, reactions, intracellular,
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month download article/chapter [2feā2s] cluster low-mr iron isolated glutaredoxin/iron clusters ironāsulfur cluster binding iron regulatory proteins intracellular cell controls article biometals aims full article pdf related subjects iron mitochondria photosystem privacy choices/manage cookies depleting cytosolic iron chelatable iron pool ļæ½chelatable iron poolā check access instant access iron responsive elements glutathione s-transferases nuclear glutathione cycle iron-citrate complexes glutaredoxin 5 deficiency cellular iron regulation expanding chemical biology european economic area naturally occurring substances equilibria involving soluble partially soluble species future drug design mammalian siderophore synthesised presently accepted levels recurrent febrile seizures riggs-gelasco pj regulators jelly rolled methodically defined quantity guinea pig reticulocytes ischemic pre conditioning dr wolfgang maret dr reinhard kissner franklināwilkins building cytoplasmic pool glutathione peroxidase activity oxygen activation reactions article hider bacterial homolog involved saccharomyces cerevisiae provide function metal trafficking vertebrate iron metabolism article log
Questions {ā}
- Kong XL, Zhou T, Neubert H, Liu Z, Hider RC (2009) 3-Hydroxy-2-(5-hydroxypentyl)-4H-chromen-4-one: a bidentate or tridentate iron(III) ligand?
- Ozer A, Bruick RK (2007) Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?
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headline:Glutathione: a key component of the cytoplasmic labile iron pool
description:The cytoplasmic labile iron pool supplies iron to the mitochondrion for heme and iron sulfur cluster synthesis and to many cytoplasmic enzymes, thereby controlling numerous metabolic reactions. Surprisingly the chemical nature of this pool has never been convincingly characterised. Here we provide evidence for iron(II)glutathione being the dominant component of this pool. We report for the first time the affinity constant for the glutathioneāiron(II) interaction and use this value to study the cytoplasmic speciation of iron(II). The formation of this complex is a major determinant of the electrode potential of the cytoplasmic ferrous iron pool, a means of selecting between iron(II) and manganese(II) and it provides a substrate for glutaredoxin/iron clusters at the dimer interface of glutaredoxins involved in the synthesis of FeāS cluster proteins.
datePublished:2011-07-17T00:00:00Z
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description:The cytoplasmic labile iron pool supplies iron to the mitochondrion for heme and iron sulfur cluster synthesis and to many cytoplasmic enzymes, thereby controlling numerous metabolic reactions. Surprisingly the chemical nature of this pool has never been convincingly characterised. Here we provide evidence for iron(II)glutathione being the dominant component of this pool. We report for the first time the affinity constant for the glutathioneāiron(II) interaction and use this value to study the cytoplasmic speciation of iron(II). The formation of this complex is a major determinant of the electrode potential of the cytoplasmic ferrous iron pool, a means of selecting between iron(II) and manganese(II) and it provides a substrate for glutaredoxin/iron clusters at the dimer interface of glutaredoxins involved in the synthesis of FeāS cluster proteins.
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