Resonance Raman spectra of rubredoxin, desulforedoxin, and the synthetic analog Fe(S2-o-xyl)2: conformational effects,
Yachandra, Vittal K., Hare Jeffrey, Moura I., and Spiro Thomas G.
, Journal of the American Chemical Society, 1983/10/01, Volume 105, Number 21, p.6455-6462, (1983)
Abstractn/a
Proteins dominate in the surface layers formed on materials exposed to extracellular polymeric substances from bacterial cultures,
Yang, Y., Wikieł A. J., Dall'agnol L. T., Eloy P., Genet M. J., Moura J. J. G., Sand W., Dupont-Gillain C. C., and Rouxhet P. G.
, Biofouling, Volume 32, p.95-108, (2016)
Conversion of desulforedoxin into a rubredoxin center,
Yu, L., Kennedy M., Czaja C., Tavares P., Moura J. J., Moura I., and Rusnak F.
, Biochem Biophys Res Commun, Feb 24, Volume 231, Number 3, p.679-82, (1997)
AbstractRubredoxin and desulforedoxin both contain an Fe(S-Cys)4 center. However, the spectroscopic properties of the center in desulforedoxin differ from rubredoxin. These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated highspin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin.
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