Functional Dissection of the Multi-Domain Di-Heme Cytochrome c550 from Thermus thermophilus (Articolo in rivista)

Type
Label
  • Functional Dissection of the Multi-Domain Di-Heme Cytochrome c550 from Thermus thermophilus (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1371/journal.pone.0055129 (literal)
Alternative label
  • Sylvain Robin, Marzia Arese, Elena Forte, Paolo Sarti, Olga Kolaj-Robin, Alessandro Giuffrè, Tewfik Soulimane (2013)
    Functional Dissection of the Multi-Domain Di-Heme Cytochrome c550 from Thermus thermophilus
    in PloS one
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sylvain Robin, Marzia Arese, Elena Forte, Paolo Sarti, Olga Kolaj-Robin, Alessandro Giuffrè, Tewfik Soulimane (literal)
Pagina inizio
  • e55129 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 8 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 11 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Chemical and Environmental Science Department, Materials and Surface Science Institute, University of Limerick, Limerick, Ireland; Department of Biochemical Sciences and Istituto Pasteur - Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italy; Consiglio Nazionale delle Ricerche Istituto di Biologia e Patologia Molecolari, Rome, Italy (literal)
Titolo
  • Functional Dissection of the Multi-Domain Di-Heme Cytochrome c550 from Thermus thermophilus (literal)
Abstract
  • In bacteria, oxidation of sulfite to sulfate, the most common strategy for sulfite detoxification, is mainly accomplished by the molybdenum-containing sulfite:acceptor oxidoreductases (SORs). Bacterial SORs are very diverse proteins; they can exist as monomers or homodimers of their core subunit, as well as heterodimers with an additional cytochrome c subunit. We have previously described the homodimeric SOR from Thermus thermophilus HB8 (SORTTHB8), identified its physiological electron acceptor, cytochrome c550, and demonstrated the key role of the latter in coupling sulfite oxidation to aerobic respiration. Herein, the role of this di-heme cytochrome c was further investigated. The cytochrome was shown to be composed of two conformationally independent domains, each containing one heme moiety. Each domain was separately cloned, expressed in E. coli and purified to homogeneity. Stopped-flow experiments showed that: i) the N-terminal domain is the only one accepting electrons from SORTTHB8; ii) the N- and C-terminal domains are in rapid redox equilibrium and iii) both domains are able to transfer electrons further to cytochrome c552, the physiological substrate of the ba3 and caa3 terminal oxidases. These findings show that cytochrome c550 functions as a electron shuttle, without working as an electron wire with one heme acting as the electron entry and the other as the electron exit site. Although contribution of the cytochrome c550 Cterminal domain to T. thermophilus sulfur respiration seems to be dispensable, we suggest that di-heme composition of the cytochrome physiologically enables storage of the two electrons generated from sulfite oxidation, thereof ensuring efficient contribution of sulfite detoxification to the respiratory chain-mediated energy generation. (literal)
Prodotto di
Autore CNR

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it