jernbinding

Jernbinding is the binding of iron ions by ligands, proteins, or materials, a concept that appears in chemistry, biochemistry, and materials science. In coordination chemistry, iron binding refers to the formation of coordination complexes in which Fe2+ or Fe3+ is held by donor atoms such as nitrogen, oxygen, or sulfur in ligands. The geometry is often octahedral, though other motifs occur, and redox chemistry between Fe2+ and Fe3+ underpins many catalytic processes.

In biology, iron binding is central to oxygen transport and storage (hemoglobin and myoglobin), electron transfer (cytochromes), and iron storage and transport (ferritin and transferrin). Non-heme iron proteins bind iron through histidine, aspartate, and carboxylate ligands; iron–sulfur clusters [Fe4S4] and other cofactors mediate electron transfer and catalysis. Bacteria and fungi produce siderophores to chelate Fe3+ with high affinity for uptake, enabling iron acquisition in iron-limited environments.

In applications, iron-binding molecules are used in chelation therapy, recycling, and water treatment. Techniques such as UV-Vis spectroscopy, electron paramagnetic resonance (EPR), and Mössbauer spectroscopy aid in studying iron-binding sites, along with crystallography and other structural methods. Proper regulation of iron binding is essential to metabolic homeostasis, and dysregulation can contribute to conditions such as iron deficiency anemia or iron overload with oxidative stress.