Purification and Preliminary Characterization of Tetraheme Cytochrome and Adenylylsulfate Reductase from the Peptidolytic Sulfate-Reducing Bacterium Desulfovibrio aminophilus DSM 12254
2005
Purification and Characterization of Proteins from Desulfovibrio aminophilus
Sample size: 310
publication
Evidence: moderate
Author Information
Author(s): Alejandro López-Cortés, Sergey Bursakov, Angelo Figueiredo, Anders E. Thapper, Smilja Todorovic, Jos J.G. Moura, Bernard Ollivier, Isabel Moura, Guy Fauque
Primary Institution: Centro de Investigaciones Biológicas del Noroeste (CIBNOR)
Conclusion
Two key proteins involved in sulfate reduction were purified and characterized from Desulfovibrio aminophilus.
Supporting Evidence
- The adenylylsulfate reductase was purified in three chromatographic steps.
- The tetraheme cytochrome c3 was also purified in three chromatographic steps.
- Both proteins were characterized using UV-visible and EPR spectroscopy.
- The tetraheme cytochrome c3 is a small monomeric protein located in the periplasmic space.
- APS reductase is a major cytoplasmic enzyme in sulfate-reducing bacteria.
Takeaway
Scientists studied a type of bacteria and found two important proteins that help it break down sulfate, which is important for its energy.
Methodology
Proteins were purified using three chromatographic steps and characterized using various spectroscopic techniques.
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