Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8XWB

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

Summary for 8XWB
Entry DOI10.2210/pdb8xwb/pdb
DescriptorFerritin heavy chain, FE (III) ION, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordshuman ferritin, metal binding protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight20579.21
Authors
Gong, W.J.,Wang, W.M.,Wang, H.F. (deposition date: 2024-01-16, release date: 2024-12-11)
Primary citationGong, W.,Wu, T.,Liu, Y.,Jiao, S.,Wang, W.,Yan, W.,Li, Y.,Liu, Y.,Zhang, Y.,Wang, H.
Insight into the photodynamic mechanism and protein binding of a nitrosyl iron-sulfur [Fe 2 S 2 (NO) 4 ] 2- cluster.
Spectrochim Acta A Mol Biomol Spectrosc, 320:124603-124603, 2024
Cited by
PubMed Abstract: 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 (MeN)[FeS(NO)] 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 at 2.040, and two other iron nitrosyl species, dinitrosyl iron units (DNICs) and mononitrosyl iron units (MNICs) with g values at 2.031 and 2.024, respectively. Moreover, the [FeS(NO)] 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.
PubMed: 38878720
DOI: 10.1016/j.saa.2024.124603
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

248942

PDB entries from 2026-02-11

PDB statisticsPDBj update infoContact PDBjnumon