PMID: 9188164Jan 1, 1997Paper

DT diaphorase exists as a dimer-tetramer equilibrium in solution

European Biophysics Journal : EBJ
O ByronJ Skelly

Abstract

The quaternary behaviour of DT diaphorase in solution has been investigated by hydrodynamics under a range of conditions. At neutral pH DT diaphorase is shown to exist as a tightly-associated homodimer in a dimer-tetramer equilibrium. Concentrations of the chaotropic agent potassium thiocyanate (KSCN) of greater than 200 mM result in irreversible loss of the FAD cofactor and denaturation of the homodimer though this agent appears to be ineffective in disrupting intermolecular association. These data conform to a model in which under extreme dissociation conditions, the folded dimer is in equilibrium with the unfolded monomer and are consistent with evidence from the X-ray structure and proposed catalytic mechanism where both monomers are catalytically interdependent.

Citations

Jan 14, 2003·Biophysical Journal·Claire J AckermanOlwyn Byron
Dec 9, 1998·International Journal of Radiation Oncology, Biology, Physics·A M RauthV Misra
Oct 18, 2000·Free Radical Biology & Medicine·A K Jaiswal
Jun 28, 2005·Biophysical Journal·Marcelo NöllmannW Marshall Stark
Jan 4, 2018·PloS One·David SiegelDavid Ross

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