Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation.

@article{Dambe2005StructureOT,
  title={Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation.},
  author={T. Dambe and A. Quentmeier and D. Rother and C. Friedrich and A. Scheidig},
  journal={Journal of structural biology},
  year={2005},
  volume={152 3},
  pages={
          229-34
        }
}
The sulfur-oxidizing enzyme system (Sox) of the chemotroph Paracoccus pantotrophus is composed of several proteins, which together oxidize hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain. The hetero-dimeric cytochrome c complex SoxXA functions as heme enzyme and links covalently the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex. Here, we report the crystal structure of the c-type… Expand
The bacterial SoxAX cytochromes
Insights into Structure and Function of the Active Site of SoxAX Cytochromes*
Redox and Chemical Activities of the Hemes in the Sulfur Oxidation Pathway Enzyme SoxAX*
Thiosulfate Dehydrogenase (TsdA) from Allochromatium vinosum
The SoxYZ Complex Carries Sulfur Cycle Intermediates on a Peptide Swinging Arm*
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References

SHOWING 1-10 OF 25 REFERENCES
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme
Cytochrome c551 from Starkeya novella
...
1
2
3
...