Structural model of the Fe-hydrogenase/cytochrome c553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations.

@article{Morelli2000StructuralMO,
  title={Structural model of the Fe-hydrogenase/cytochrome c553 complex combining transverse relaxation-optimized spectroscopy experiments and soft docking calculations.},
  author={Xavier Morelli and Mirjam Czjzek and Claude E. Hatchikian and Olivier Bornet and Juan C Fontecilla-Camps and N{\'u}{\~n}ez Palma and Jos{\'e} J. G. Moura and Françoise Guerlesquin},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 30},
  pages={
          23204-10
        }
}
Fe-hydrogenase is a 54-kDa iron-sulfur enzyme essential for hydrogen cycling in sulfate-reducing bacteria. The x-ray structure of Desulfovibrio desulfuricans Fe-hydrogenase has recently been solved, but structural information on the recognition of its redox partners is essential to understand the structure-function relationships of the enzyme. In the present work, we have obtained a structural model of the complex of Fe-hydrogenase with its redox partner, the cytochrome c(553), combining… CONTINUE READING
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