Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study (Articolo in rivista)

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  • Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Alternative label
  • Bolli, A; Ciaccio, C; Coletta, M; Nardini, M; Bolognesi, M; Pesce, A; Guertin, M; Visca, P; Ascenzi, P (2008)
    Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bolli, A; Ciaccio, C; Coletta, M; Nardini, M; Bolognesi, M; Pesce, A; Guertin, M; Visca, P; Ascenzi, P (literal)
Pagina inizio
  • 633 (literal)
Pagina fine
  • 645 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 275 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • \"[Bolli, Alessandro; Visca, Paolo; Ascenzi, Paolo] Univ Roma Tre, Dipartimento Biol, I-00146 Rome, Italy; [Bolli, Alessandro; Visca, Paolo; Ascenzi, Paolo] Univ Roma Tre, Lab Interdept Microscopia Elettron, I-00146 Rome, Italy; [Ciaccio, Chiara; Coletta, Massimo] Univ Roma Tre, Dipartimento Med Sperimentale & Sci Biochim, Rome, Italy; [Ciaccio, Chiara; Coletta, Massimo] Consorzio Interuniv Ric Chim Met Sistemi Biol, Bari, Italy; [Nardini, Marco; Bolognesi, Martino] Univ Milan, Dipartimento Sci Biomol & Biotecnol, I-20122 Milan, Italy; [Nardini, Marco; Bolognesi, Martino] Univ Milan, CNR INFM, I-20122 Milan, Italy; [Pesce, Alessandra] Univ Genoa, Dipartmento Fis, CNR INFM, Genoa, Italy; [Pesce, Alessandra] Univ Genoa, Ctr Eccellenza Ric Biomed, Genoa, Italy; [Guertin, Michel] Univ Laval, Fac Sci & Genie, Dept Biochim & Microbiol, Quebec City, PQ G1K 7P4, Canada; [Visca, Paolo; Ascenzi, Paolo] IRCCS Lazzaro Spallanzani, Ist Nazl Malattie Infett, Rome, Italy (literal)
Titolo
  • Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study (literal)
Abstract
  • \"Campylobacter jejuni hosts two hemoglobins (Hbs). The Camplylobacter jejuni single-domain Hb (called Cgb) is homologous to the globin domain of flavohemoglobin, and it has been proposed to protect the bacterium against nitrosative stress. The second Hb is called Ctb (hereafter Cj-trHbP), belongs to truncated Hb group III, and has been hypothesized to be involved in O-2 chemistry. Here, the kinetics and thermodynamics of cyanide binding to ferric and ferrous Cj-trHbP [Cj-trHbP(III) and Cj-trHbP(II), respectively] are reported and analyzed in parallel with those of related heme proteins, with particular reference to those from Mycobacterium tuberculosis. The affinity of cyanide for Cj-trHbP(II) is higher than that reported for any known (in)vertebrate globin by more than three orders of magnitude (K = 1.2 x 10(-6) M). This can be fully attributed to the highest (ever observed for a ferrous Hb) cyanide-binding association rate constant (k(on) = 3.3 x 10(3) M-1.s(-1)), even though the binding process displays a rate-limiting step (k(max) = 9.1 s(-1)). Cj-trHbP(III) shows a very high affinity for cyanide (L = 5.8 x 10(-9) M); however, cyanide association kinetics are independent of cyanide concentration, displaying a rate-limiting step (l(max) = 2.0 x 10(-3) s(-1)). Values of the first-order rate constant for cyanide dissociation from Cj-trHbP(II)-cyanide and Cj-trHbP(III)-cyanide (k(off) =5.0 x 10(-3) s(-1) and l(off) >= 1 x 10(-4) s(-1), respectively) are similar to those reported for (in)vertebrate globins. The very high affinity of cyanide for Cj-trHbP(II), reminiscent of that of horseradish peroxidase(II), suggests that this globin may participate in cyanide detoxification.\" (literal)
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