Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - A comparative study

Alessandro Bolli, Chiara Ciaccio, Massimo Coletta, Marco Nardini, Martino Bolognesi, Alessandra Pesce, Michel Guertin, Paolo Visca, Paolo Ascenzi

Research output: Contribution to journalArticle

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 × 10-6 m). This can be fully attributed to the highest (ever observed for a ferrous Hb) cyanide-binding association rate constant (kon = 3.3 × 103 m-1·s-1), even though the binding process displays a rate-limiting step (kmax = 9.1 s -1). Cj-trHbP(III) shows a very high affinity for cyanide (L = 5.8 × 10-9 m); however, cyanide association kinetics are independent of cyanide concentration, displaying a rate-limiting step (l max = 2.0 × 10-3 s-1). Values of the first-order rate constant for cyanide dissociation from Cj-trHbP(II)-cyanide and Cj-trHbP(III)-cyanide (koff =5.0 × 10-3 s -1 and loff ≥ 1 × 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.

Original languageEnglish
Pages (from-to)633-645
Number of pages13
JournalFEBS Journal
Volume275
Issue number4
DOIs
Publication statusPublished - Feb 2008

Fingerprint

Truncated Hemoglobins
Campylobacter jejuni
Cyanides
Globins
Vertebrates
Rate constants
hemoglobin P
Association reactions
Hemeproteins
Detoxification
Kinetics
Horseradish Peroxidase
Thermodynamics
Mycobacterium tuberculosis

Keywords

  • Campylobacter jejuni truncated hemoglobin P
  • Cyanide binding
  • Kinetics
  • Mycobacterium tuberculosis truncated hemoglobin N and O
  • Thermodynamics

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - A comparative study. / Bolli, Alessandro; Ciaccio, Chiara; Coletta, Massimo; Nardini, Marco; Bolognesi, Martino; Pesce, Alessandra; Guertin, Michel; Visca, Paolo; Ascenzi, Paolo.

In: FEBS Journal, Vol. 275, No. 4, 02.2008, p. 633-645.

Research output: Contribution to journalArticle

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', FEBS Journal, vol. 275, no. 4, pp. 633-645. https://doi.org/10.1111/j.1742-4658.2007.06223.x
Bolli, Alessandro ; Ciaccio, Chiara ; Coletta, Massimo ; Nardini, Marco ; Bolognesi, Martino ; Pesce, Alessandra ; Guertin, Michel ; Visca, Paolo ; Ascenzi, Paolo. / Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - A comparative study. In: FEBS Journal. 2008 ; Vol. 275, No. 4. pp. 633-645.
@article{d801316dabb7441bbd15a821229d39bf,
title = "Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - A comparative study",
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 × 10-6 m). This can be fully attributed to the highest (ever observed for a ferrous Hb) cyanide-binding association rate constant (kon = 3.3 × 103 m-1·s-1), even though the binding process displays a rate-limiting step (kmax = 9.1 s -1). Cj-trHbP(III) shows a very high affinity for cyanide (L = 5.8 × 10-9 m); however, cyanide association kinetics are independent of cyanide concentration, displaying a rate-limiting step (l max = 2.0 × 10-3 s-1). Values of the first-order rate constant for cyanide dissociation from Cj-trHbP(II)-cyanide and Cj-trHbP(III)-cyanide (koff =5.0 × 10-3 s -1 and loff ≥ 1 × 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.",
keywords = "Campylobacter jejuni truncated hemoglobin P, Cyanide binding, Kinetics, Mycobacterium tuberculosis truncated hemoglobin N and O, Thermodynamics",
author = "Alessandro Bolli and Chiara Ciaccio and Massimo Coletta and Marco Nardini and Martino Bolognesi and Alessandra Pesce and Michel Guertin and Paolo Visca and Paolo Ascenzi",
year = "2008",
month = "2",
doi = "10.1111/j.1742-4658.2007.06223.x",
language = "English",
volume = "275",
pages = "633--645",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "4",

}

TY - JOUR

T1 - Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - A comparative study

AU - Bolli, Alessandro

AU - Ciaccio, Chiara

AU - Coletta, Massimo

AU - Nardini, Marco

AU - Bolognesi, Martino

AU - Pesce, Alessandra

AU - Guertin, Michel

AU - Visca, Paolo

AU - Ascenzi, Paolo

PY - 2008/2

Y1 - 2008/2

N2 - 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 × 10-6 m). This can be fully attributed to the highest (ever observed for a ferrous Hb) cyanide-binding association rate constant (kon = 3.3 × 103 m-1·s-1), even though the binding process displays a rate-limiting step (kmax = 9.1 s -1). Cj-trHbP(III) shows a very high affinity for cyanide (L = 5.8 × 10-9 m); however, cyanide association kinetics are independent of cyanide concentration, displaying a rate-limiting step (l max = 2.0 × 10-3 s-1). Values of the first-order rate constant for cyanide dissociation from Cj-trHbP(II)-cyanide and Cj-trHbP(III)-cyanide (koff =5.0 × 10-3 s -1 and loff ≥ 1 × 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.

AB - 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 × 10-6 m). This can be fully attributed to the highest (ever observed for a ferrous Hb) cyanide-binding association rate constant (kon = 3.3 × 103 m-1·s-1), even though the binding process displays a rate-limiting step (kmax = 9.1 s -1). Cj-trHbP(III) shows a very high affinity for cyanide (L = 5.8 × 10-9 m); however, cyanide association kinetics are independent of cyanide concentration, displaying a rate-limiting step (l max = 2.0 × 10-3 s-1). Values of the first-order rate constant for cyanide dissociation from Cj-trHbP(II)-cyanide and Cj-trHbP(III)-cyanide (koff =5.0 × 10-3 s -1 and loff ≥ 1 × 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.

KW - Campylobacter jejuni truncated hemoglobin P

KW - Cyanide binding

KW - Kinetics

KW - Mycobacterium tuberculosis truncated hemoglobin N and O

KW - Thermodynamics

UR - http://www.scopus.com/inward/record.url?scp=38549143584&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=38549143584&partnerID=8YFLogxK

U2 - 10.1111/j.1742-4658.2007.06223.x

DO - 10.1111/j.1742-4658.2007.06223.x

M3 - Article

C2 - 18190529

AN - SCOPUS:38549143584

VL - 275

SP - 633

EP - 645

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 4

ER -