Extremophilic hemoglobins: The structure of Shewanella benthica truncated hemoglobin N

Martinez Grundman J, Schultz T, Schlessman J, Johnson E, Gillilan R, Lecomte J, Journal of Biological Chemistry :108223 (2025) DOI

SASDWW4 – Shewanella benthica hemoglobin K111I 50 MPa

Group 1 truncated hemoglobin (C51S, C71S, K111I)
MWexperimental 9 kDa
MWexpected 13 kDa
VPorod 24 nm3
log I(s) 1.13×10-1 1.13×10-2 1.13×10-3 1.13×10-4
Group 1 truncated hemoglobin (C51S, C71S, K111I) small angle scattering data  s, nm-1
ln I(s)
Group 1 truncated hemoglobin (C51S, C71S, K111I) Guinier plot ln 1.14×10-1 Rg: 1.6 nm 0 (1.6 nm)-2 s2
(sRg)2I(s)/I(0)
Group 1 truncated hemoglobin (C51S, C71S, K111I) Kratky plot 1.104 0 3 sRg
Dmax: 6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Shewanella benthica hemoglobin K111I 50 MPa in 14 mM Tris, 6 mM potassium phosphate, pH 7 were collected on the ID7A1 BioSAXS / HP-Bio Beamline beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Eiger 4M detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.0883 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 23°C. Four successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

50 MPa hydrostatic pressure.

Group 1 truncated hemoglobin (C51S, C71S, K111I) (K111I S2SbHbN)
Mol. type   Protein
Organism   Shewanella benthica KT99
Olig. state   Unknown
Mon. MW   12.8 kDa
 
UniProt   A9DF82 (2-117)
Sequence   FASTA