8xwb

Crystal structure of dinitrosyl iron units binding with human heavy chain Ferritin

spinqualitylabelsall models 8xwb, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xwb is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: CL, FE, MG, NO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FRIH_HUMAN Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). Publication Abstract from PubMed Iron-sulfur cluster conversion and nitrosyl modification are involved in regulating their functions and play critical roles in signaling for biological systems. Hereby, the photo-induced dynamic process of (Me(4)N)(2)[Fe(2)S(2)(NO)(4)] was monitored using time-resolved electron paramagnetic resonance (EPR) spectra, MS spectra and cellular imaging methods. Photo-irradiation and the solvent affect the reaction rates and products. Spectroscopic and kinetic studies have shown that the process involves at least three intermediates: spin-trapped NO free radical species with a g(av) at 2.040, and two other iron nitrosyl species, dinitrosyl iron units (DNICs) and mononitrosyl iron units (MNICs) with g(av) values at 2.031 and 2.024, respectively. Moreover, the [Fe(2)S(2)(NO)(4)](2-) cluster could bind with ferritin and decompose gradually, and a binding state of dinitrosyl iron coordinated with Cys102 of the recombinant human heavy chain ferritin (rHuHF) was finally formed. This study provides insight into the photodynamic mechanism of nitrosyl iron - sulfur clusters to improve the understanding of physiological activity. Insight into the photodynamic mechanism and protein binding of a nitrosyl iron-sulfur [Fe(2)S(2)(NO)(4)](2-) cluster.,Gong W, Wu T, Liu Y, Jiao S, Wang W, Yan W, Li Y, Liu Y, Zhang Y, Wang H Spectrochim Acta A Mol Biomol Spectrosc. 2024 Nov 5;320:124603. doi: , 10.1016/j.saa.2024.124603. Epub 2024 Jun 5. PMID:38878720 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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