Transient iron coordination sites in proteins: Exploiting the dual nature of paramagnetic NMR

摘要: Abstract We provide here an historical perspective of NMR applied to iron-containing proteins. At first, the field developed using paramagnetic NMR: 1H spectra heme and FeS proteins were used as clear spectroscopic fingerprints electronic structure metal ion its inner outer coordination spheres. Starting 1994, metalloproteins was focused more on protein part determination 3D structures in solution small achieved; observables exploited non-conventional constraints. With time, has gained attention a methodology monitor protein–protein interactions, becoming unique tool learn about interaction surfaces weak transient complexes. The recent interest understanding homeostatis cofactor assembly led renewed application (i) tool, characterize novel binding site centers where is no integral but rather chemical entity that be transferred along trafficking pathways or undergo specific reactions (ii) structural method for definition metal-mediated interactions. reported case examples cover bacterial acquisition system, cytosolic mitochondrial cluster machineries eukaryotic iron-storage ferritin.