A hidden property of the iron-sulfur protein in the mononuclear iron-bound state: species-dependent structural ordering induced by magnetic fields.

Arai S, Soga S, Hirai M, Kobayashi R, Masai H, Kimura K, Maeda K, Nagashima H, FEBS J (2025) Europe PMC

SASDUJ9 – Mononuclear iron bound form of human ISCA1 under 180 mT magnetic field for 60 min

Human Iron-sulfur cluster assembly 1 homolog, mitochondrial
MWexperimental 14 kDa
MWexpected 14 kDa
VPorod 66 nm3
log I(s) 1.86×10-1 1.86×10-2 1.86×10-3 1.86×10-4
Human Iron-sulfur cluster assembly 1 homolog, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Human Iron-sulfur cluster assembly 1 homolog, mitochondrial Guinier plot ln 1.86×10-1 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Human Iron-sulfur cluster assembly 1 homolog, mitochondrial Kratky plot 1.104 0 √3 sRg
p(r)
Human Iron-sulfur cluster assembly 1 homolog, mitochondrial pair distance distribution function Rg: 3.2 nm 0 Dmax: 11.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Mononuclear iron bound form of human ISCA1 under 180 mT magnetic field for 60 min in 20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH 8 were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK) storage ring (Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.00 mg/ml was measured at 20°C. One 60 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Human Iron-sulfur cluster assembly 1 homolog, mitochondrial (hsISCA1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   14.4 kDa
 
UniProt   Q9BUE6 (2-129)
Sequence   FASTA