Search

Structural and charge interaction analyses of the binding site of the aspartate 95 mutants of the Desulfovibrio vulgaris flavodoxin reveals the role played by the hydrogen bonding in the modulation of the redox potentials of the bound flavodoxin, particularly the carboxylate group of the mutant.

A study was conducted to understand the kinetic mechanism related to the role of structurally homologous flavoproteins photolyases and cryptochromes (CRY) towards UV-damaged DNA repair by photoinduced electron transfer from their FAD cofactor. The results obtained offer insight into the kinetic tuning of the rates of electron transfer which would play a function-defining role in photolyases and cryptochromes.

A study was conducted to analyze pH-dependent spectroscopic changes related to the hydroquinone of FMN in flavodoxins. Flavodoxin from D. vulgaris was determined as the recombinant protein. Results indicated that a decrease in pH promotes a change in the electronic structure of the reduced flavin resulting from changes in the ionization state of the flavin and in the hydrogen-bonding network around the flavin.

A quantitative J-correlation pulse sequence is described that allows simultaneous determination of one-bond and two-bond nitrogen-carbon coupling constants for protonated or deuterated proteins. Coupling constants are calculated from volume ratios between cross peaks and reference axial peaks observed in a single 3D spectrum. Accurate backbone 1JNC′, 1JNCα, and 2JNCα coupling constants are obtained for the two [15N;13C]-labeled, medium-sized proteins flavodoxin and xylanase and for the [2H;15N;13C]-labeled, large protein DFPase. A dependence of one-bond and two-bond JNCα values on protein backbone ψ torsion angles is readily apparent, in agreement with previously found correlations. In addition, the experiment is performed on isotropic as well as aligned protein to measure associated 15N-13C residual dipolar couplings. [ABSTRACT FROM AUTHOR]

Reports on the complete assignment of the chemical shifts for the hydroquinone of Desulfovibrio vulgaris wild-type flavodoxin and the deposition of the chemical shifts for the oxidized and fully reduced states. Comparison of the chemical shift differences between these two redox states; Extent of assignment and data deposition.