Robin 2011 J Bacteriol: Difference between revisions
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|authors=Robin S, Arese M, Forte E, Sarti P, Giuffre A, Soulimane T | |authors=Robin S, Arese M, Forte E, Sarti P, Giuffre A, Soulimane T | ||
|year=2011 | |year=2011 | ||
|journal=J | |journal=J Bacteriol | ||
|abstract=Sulfite, produced for instance during amino acid metabolism, is a very reactive and toxic compound. Various detoxification mechanisms exist, but sulfite oxidoreductases (SORs) are one of the major actors in sulfite remediation in bacteria and animals. Here we describe the existence of an operon in the extreme thermophilic bacterium Thermus thermophilus HB8 encoding both a SOR and a diheme c-type cytochrome. The in vitro analysis clearly showed that the newly identified cytochrome c₅₅₀ acts as an acceptor of the electrons generated by the SOR enzyme during the oxidation of sulfite. The electrons are then rapidly shuttled via cytochrome c₅₅₂ to the terminal ba₃- and caa₃-type oxidases, thereby unveiling a novel electron transfer pathway, linking sulfite oxidation to oxygen reduction in T. thermophilus: sulfite → SOR(HB8) → cytochrome c₅₅₀ → cytochrome c₅₅₂ → ba₃ oxidase/caa₃ oxidase → O₂. The description of the complete pathway reveals that electrons generated during sulfite oxidation by the SOR are funneled into the respiratory chain, participating in the energy production of T. thermophilus. | |abstract=Sulfite, produced for instance during amino acid metabolism, is a very reactive and toxic compound. Various detoxification mechanisms exist, but sulfite oxidoreductases (SORs) are one of the major actors in sulfite remediation in bacteria and animals. Here we describe the existence of an operon in the extreme thermophilic bacterium Thermus thermophilus HB8 encoding both a SOR and a diheme c-type cytochrome. The in vitro analysis clearly showed that the newly identified cytochrome c₅₅₀ acts as an acceptor of the electrons generated by the SOR enzyme during the oxidation of sulfite. The electrons are then rapidly shuttled via cytochrome c₅₅₂ to the terminal ba₃- and caa₃-type oxidases, thereby unveiling a novel electron transfer pathway, linking sulfite oxidation to oxygen reduction in T. thermophilus: sulfite → SOR(HB8) → cytochrome c₅₅₀ → cytochrome c₅₅₂ → ba₃ oxidase/caa₃ oxidase → O₂. The description of the complete pathway reveals that electrons generated during sulfite oxidation by the SOR are funneled into the respiratory chain, participating in the energy production of T. thermophilus. | ||
|keywords=sulfite oxidoreductase, Thermus thermophilus | |keywords=sulfite oxidoreductase, Thermus thermophilus | ||
Revision as of 23:03, 19 December 2011
| Robin S, Arese M, Forte E, Sarti P, Giuffrè A, Soulimane T (2011) A sulfite respiration pathway from Thermus thermophilus and the key role of newly identified cytochrome c550. J Bacteriol 193: 3988-3997. |
Robin S, Arese M, Forte E, Sarti P, Giuffre A, Soulimane T (2011) J Bacteriol
Abstract: Sulfite, produced for instance during amino acid metabolism, is a very reactive and toxic compound. Various detoxification mechanisms exist, but sulfite oxidoreductases (SORs) are one of the major actors in sulfite remediation in bacteria and animals. Here we describe the existence of an operon in the extreme thermophilic bacterium Thermus thermophilus HB8 encoding both a SOR and a diheme c-type cytochrome. The in vitro analysis clearly showed that the newly identified cytochrome c₅₅₀ acts as an acceptor of the electrons generated by the SOR enzyme during the oxidation of sulfite. The electrons are then rapidly shuttled via cytochrome c₅₅₂ to the terminal ba₃- and caa₃-type oxidases, thereby unveiling a novel electron transfer pathway, linking sulfite oxidation to oxygen reduction in T. thermophilus: sulfite → SOR(HB8) → cytochrome c₅₅₀ → cytochrome c₅₅₂ → ba₃ oxidase/caa₃ oxidase → O₂. The description of the complete pathway reveals that electrons generated during sulfite oxidation by the SOR are funneled into the respiratory chain, participating in the energy production of T. thermophilus. • Keywords: sulfite oxidoreductase, Thermus thermophilus
• O2k-Network Lab: IT_Roma_Sarti P
Labels:
Organism: Bacteria"Bacteria" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Enzyme: Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
HRR: Oxygraph-2k
