Biophysical and structural characterization of a sequence-diverse set of solute-binding proteins for aromatic compounds.

ABSTRACT: Rhodopseudomonas palustris metabolizes aromatic compounds derived from lignin degradation products and has the potential for bioremediation of xenobiotic compounds. We recently identified four possible solute-binding proteins in R. palustris that demonstrated binding to aromatic lignin monomers. Characterization of these proteins in the absence and presence of the aromatic ligands will provide unprecedented insights into the specificity and mode of aromatic ligand binding in solute-binding proteins. Here, we report the thermodynamic and structural properties of the proteins with aromatic ligands using isothermal titration calorimetry, small/wide angle x-ray scattering, and theoretical predictions. The proteins exhibit high affinity for the aromatic substrates with dissociation constants in

SUBMITTER: Pietri R 

PROVIDER: S-EPMC3390649 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature