Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate

Paolo Ascenzi, Alessio Bocedi, Martino Bolognesi, Giulia Fabozzi, Mario Milani, Paolo Visca

Research output: Contribution to journalArticle

Abstract

Ferrous oxygenated (Fe(II)O2) hemoglobins (Hb's) and myoglobins (Mb's) have been shown to react very rapidly with NO, yielding NO 3 - and the ferric heme-protein derivative (Fe(III)), by means of the ferric heme-bound peroxynitrite intermediate (Fe(III)OONO), according to the minimum reaction scheme:Fe(II)O2+NO→konFe(III) OONO→hFe(III)+NO3-For most Hb's and Mb's, the first step (indicated by kon) is rate limiting, the overall reaction following a bimolecular behavior. By contrast, the rate of isomerization and dissociation of Fe(III)OONO (indicated by h) is rate limiting in NO scavenging by Fe(II)O2 murine neuroglobin, thus the overall reaction follows a monomolecular behavior. Here, we report the characterization of the NO scavenging reaction by Fe(II)O2 truncated Hb GlbO from Mycobacterium leprae. Values of kon (=2.1 × 106 M-1 s-1) and h (=3.4 s-1) for NO scavenging by Fe(II)O2 M. leprae GlbO have been determined at pH 7.3 and 20.0°C, the rate of Fe(III)OONO decay (h) is rate limiting. The Fe(III)OONO intermediate has been characterized by optical absorption spectroscopy in the Soret region. These results have been analyzed in parallel with those of monomeric and tetrameric globins as well as of flavoHb and discussed with regard to the three-dimensional structure of mycobacterial truncated Hbs and their proposed role in protection from nitrosative stress.

Original languageEnglish
Pages (from-to)450-456
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume339
Issue number1
DOIs
Publication statusPublished - Jan 6 2006

Fingerprint

Mycobacterium leprae
Peroxynitrous Acid
Myoglobin
Scavenging
Heme
Nitric Oxide
Hemoglobins
Hemeproteins
Globins
Spectrum Analysis
Isomerization
Absorption spectroscopy
Light absorption
Derivatives
neuroglobin

Keywords

  • Kinetics of heme-Fe(II)O oxidation by NO
  • Mycobacterium leprae GlbO
  • NO scavenging
  • NO-mediated heme-Fe(II)O oxidation
  • Optical absorption spectroscopy
  • Transient heme-Fe(III)OONO complex formation and decay
  • Truncated hemoglobin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate. / Ascenzi, Paolo; Bocedi, Alessio; Bolognesi, Martino; Fabozzi, Giulia; Milani, Mario; Visca, Paolo.

In: Biochemical and Biophysical Research Communications, Vol. 339, No. 1, 06.01.2006, p. 450-456.

Research output: Contribution to journalArticle

Ascenzi, Paolo ; Bocedi, Alessio ; Bolognesi, Martino ; Fabozzi, Giulia ; Milani, Mario ; Visca, Paolo. / Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate. In: Biochemical and Biophysical Research Communications. 2006 ; Vol. 339, No. 1. pp. 450-456.
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abstract = "Ferrous oxygenated (Fe(II)O2) hemoglobins (Hb's) and myoglobins (Mb's) have been shown to react very rapidly with NO, yielding NO 3 - and the ferric heme-protein derivative (Fe(III)), by means of the ferric heme-bound peroxynitrite intermediate (Fe(III)OONO), according to the minimum reaction scheme:Fe(II)O2+NO→konFe(III) OONO→hFe(III)+NO3-For most Hb's and Mb's, the first step (indicated by kon) is rate limiting, the overall reaction following a bimolecular behavior. By contrast, the rate of isomerization and dissociation of Fe(III)OONO (indicated by h) is rate limiting in NO scavenging by Fe(II)O2 murine neuroglobin, thus the overall reaction follows a monomolecular behavior. Here, we report the characterization of the NO scavenging reaction by Fe(II)O2 truncated Hb GlbO from Mycobacterium leprae. Values of kon (=2.1 × 106 M-1 s-1) and h (=3.4 s-1) for NO scavenging by Fe(II)O2 M. leprae GlbO have been determined at pH 7.3 and 20.0°C, the rate of Fe(III)OONO decay (h) is rate limiting. The Fe(III)OONO intermediate has been characterized by optical absorption spectroscopy in the Soret region. These results have been analyzed in parallel with those of monomeric and tetrameric globins as well as of flavoHb and discussed with regard to the three-dimensional structure of mycobacterial truncated Hbs and their proposed role in protection from nitrosative stress.",
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AU - Ascenzi, Paolo

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AU - Milani, Mario

AU - Visca, Paolo

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N2 - Ferrous oxygenated (Fe(II)O2) hemoglobins (Hb's) and myoglobins (Mb's) have been shown to react very rapidly with NO, yielding NO 3 - and the ferric heme-protein derivative (Fe(III)), by means of the ferric heme-bound peroxynitrite intermediate (Fe(III)OONO), according to the minimum reaction scheme:Fe(II)O2+NO→konFe(III) OONO→hFe(III)+NO3-For most Hb's and Mb's, the first step (indicated by kon) is rate limiting, the overall reaction following a bimolecular behavior. By contrast, the rate of isomerization and dissociation of Fe(III)OONO (indicated by h) is rate limiting in NO scavenging by Fe(II)O2 murine neuroglobin, thus the overall reaction follows a monomolecular behavior. Here, we report the characterization of the NO scavenging reaction by Fe(II)O2 truncated Hb GlbO from Mycobacterium leprae. Values of kon (=2.1 × 106 M-1 s-1) and h (=3.4 s-1) for NO scavenging by Fe(II)O2 M. leprae GlbO have been determined at pH 7.3 and 20.0°C, the rate of Fe(III)OONO decay (h) is rate limiting. The Fe(III)OONO intermediate has been characterized by optical absorption spectroscopy in the Soret region. These results have been analyzed in parallel with those of monomeric and tetrameric globins as well as of flavoHb and discussed with regard to the three-dimensional structure of mycobacterial truncated Hbs and their proposed role in protection from nitrosative stress.

AB - Ferrous oxygenated (Fe(II)O2) hemoglobins (Hb's) and myoglobins (Mb's) have been shown to react very rapidly with NO, yielding NO 3 - and the ferric heme-protein derivative (Fe(III)), by means of the ferric heme-bound peroxynitrite intermediate (Fe(III)OONO), according to the minimum reaction scheme:Fe(II)O2+NO→konFe(III) OONO→hFe(III)+NO3-For most Hb's and Mb's, the first step (indicated by kon) is rate limiting, the overall reaction following a bimolecular behavior. By contrast, the rate of isomerization and dissociation of Fe(III)OONO (indicated by h) is rate limiting in NO scavenging by Fe(II)O2 murine neuroglobin, thus the overall reaction follows a monomolecular behavior. Here, we report the characterization of the NO scavenging reaction by Fe(II)O2 truncated Hb GlbO from Mycobacterium leprae. Values of kon (=2.1 × 106 M-1 s-1) and h (=3.4 s-1) for NO scavenging by Fe(II)O2 M. leprae GlbO have been determined at pH 7.3 and 20.0°C, the rate of Fe(III)OONO decay (h) is rate limiting. The Fe(III)OONO intermediate has been characterized by optical absorption spectroscopy in the Soret region. These results have been analyzed in parallel with those of monomeric and tetrameric globins as well as of flavoHb and discussed with regard to the three-dimensional structure of mycobacterial truncated Hbs and their proposed role in protection from nitrosative stress.

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