@article {2400, title = {Broad-temperature range spectroscopy of the two-centre modular redox metalloprotein Desulfovibrio desulfuricans desulfoferrodoxin}, journal = {Dalton Transactions}, number = {17}, year = {2003}, note = {

Times Cited: 2

}, month = {Sep 7}, pages = {3328-3338}, abstract = {

The electronic-vibrational couplings of the two-centre non-heme iron protein Desulfovibrio desulfuricans desulfoferrodoxin (DFx) in three oxidation states, i.e. fully oxidised (grey), half-oxidised (pink), and fully reduced (colourless), have been investigated by variable temperature (VT) UV/VIS, MCD, CD, and EPR spectroscopy. The UV/VIS spectra of grey DFx at room temperature is characterised by broad charge transfer (CT) transitions associated with oxidised centre 1 (495 and 368 nm) and II (335 and 635 nm). The transitions are resolved at 78 K, substantiated by VT-MCD and -CD. The data offer novel information about the electronic-vibrational couplings of the transitions. Multiphonon bandshape analysis discloses strong contributions from both local Fe-S and S-C stretching and solvent/protein modes. A number of transitions are blue- or red-shifted compared with monomeric desulforedoxin, superoxide reductase or dismutase, and cloned Desulfovibrio vulgaris DFx fragments. Conversion from grey to pink DFx is accompanied by drastic electronic-vibrational changes of both centres. The data suggest that electron transfer and optical CT-transitions of DFx are controlled by environmental reorganization in the whole region between the metal centres.

}, isbn = {1477-9226}, url = {http://dx.doi.org/10.1039/b303656a}, author = {Andersen, N. H. and Harnung, S. E. and Trabjerg, I. and Moura, I. and Moura, J. J. G. and Ulstrup, J.} }