Themed collection Iron in Biology

Welcome to this Metallomics themed collection on iron in biology, guest edited by Vincenzo Abbate and Robert Hider.

Widely divergent views emerge on the central steps in the uptake, catalytic oxidation, and transfer of iron ions by ferritin.

Vertebrate red blood cells (RBCs) arise from erythroblasts in the human bone marrow through a process known as erythropoiesis.

Iron plays a crucial role in biochemistry and is an essential micronutrient for plants and humans alike. Recent progress in the field has led to a better understanding of iron homeostasis in plants, and aided the production of high iron crops for improved human nutrition.

There are numerous blood-based biomarkers for assessing iron stores, but all come with certain limitations.

Atopic individuals are often iron-deficient and tend to develop a Th2 dominant immune response, resulting in hyperresponsiveness to harmless antigens, termed allergens.

Iron is an essential redox element that functions as a cofactor in many metabolic pathways.

The transferrin receptor (TfR1), which mediates cellular iron uptake through clathrin-dependent endocytosis of iron-loaded transferrin, plays a key role in iron homeostasis.

Iron-containing enzymes such as heme enzymes play crucial roles in biological systems.

The structural and chemical similarities between manganese (Mn) and iron (Fe) allow the two metals to interact with each other in biological systems.

The biosyntheses of a family of enterobactin variants – amino acid substitution, insertion, and derivatization, and macrolactone expansion – is reviewed.

Iron efflux transporters play a critical role in protecting cells from iron intoxication.

Two pairs of Fe(II) (orange) tightly bound to two putative Fe(II) bowls (forest green) may bridge neighboring protein residues (red) in each gating ring of Slo1 BK_Ca for channel closure. The binding of Ca(II) (green) to the gating ring or the binding of carbon monoxide to either binuclear Fe(II) bowl may disrupt the Fe(II) bridge for channel opening but retain Fe(II) in the bowl.

High-affinity Zn(II) bridging C1344 of nucleotide-binding domain 2 (NBD2) with E402 of NBD1, D173 of intracellular loop1 (ICL1) and the adenine group of ATP at the degenerate site may stimulate channel opening of poorly-phosphorylated human CFTR once the high-affinity Fe(III) site at the interface of the regulatory (R) domain and ICL3 is removed.

A single nucleotide polymorphism (rs10455) in the last exon of the Dcytb gene in C282Y hemochromatosis subjects exhibited increased ferric reductase activity in transgenic CHO cells.

Much evidence indicates that iron stored in ferritin is mobilized through protein degradation in lysosomes, but concerns about this process have lingered, and mechanistic details of its aspects are lacking.

Cytochrome P450 enzymes (P450) play essential roles in redox metabolism in all domains of life including detoxification reactions and sterol biosynthesis.

Dietary iron overload affects liver metabolic homeostasis, reducing mitochondrial respiratory capacity, and increasing reactive oxygen species (ROS) production, in a strain-dependent manner.

Systematic mutation of Cia2's conserved motifs reveals the Cia1 binding site and suggests Cia2 has an additional, currently cryptic, function.

Tyr58 and Trp133 play key roles in the formation and decay of the Tyr25 radical species of E. coli BFR.

Sickle cell disease (SCD) is an inherited blood disorder caused by a β globin gene mutation of hemoglobin (HbS). TD-1 enhances oxygen affinity and prevents sickling of SS RBCs as well as providing protection against iron oxidation.

Grx4 forms a cysteine-ligated [2Fe–2S] binding complex with the transcriptional repressor Php4 to regulate transcription of iron utilization genes.

The metal-chelating host-defense protein human calprotectin promotes the reduction of Fe(III) to Fe(II).

Investigation of the mechanisms of mitochondrial metal binding to frataxin in vitro.

BTS family members negatively regulate the Fe deficiency response; mutants have increased Fe levels and tolerance to Fe deficiency.

One dual-function (2) and one first-generation (9) conjugate of the Fe(III) chelator desferrioxamine B (DFOB, 1) showed significant rescue of neurons in the MPTP mouse model of Parkinson's disease.

During Fe–S cluster synthesis, oligomerization of the scaffold enables stable contacts with the iron- and sulfur-donor, with structural features predicted to facilitate cluster assembly and delivery.

Flexible aspartates propel iron to the ferroxidation centre (FOC) in miniferritins.

The BfrB:Bfd interaction enables a dynamic equilibrium between free cytosolic Fe²⁺ and Fe³⁺ in BfrB, which functions as a buffer to oppose large fluctuations of free cytosolic Fe²⁺.