Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative

A spectroscopic and thermodynamic Study

Paolo Ascenzi, Massimo Coletta, Roberto Santucci, Francesca Polizio, Alessandro Desideri

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative has been investigated quantitatively by EPR and absorbance spectroscopy. The X-band EPR spectra and the absorption spectra in the Soret region of the nitrosylated derivative of ferrous native and carboxymethylated cytochrome c display the same basic characteristics reported for the beef heart cytochrome a3 in cytochrome c oxidase, and horseradish and baker's yeast cytochrome c peroxidase, as well as the high affinity form of oxygen carrying proteins. Values of the dissociation equilibrium constant for nitrosylation of ferrous native and carboxymethylated cytochrome c are 8.2 × 10-6 M and ≤ 5 × 10-8 M, respectively, at pH 7.0 and 10°C. The results here reported represent clearcut evidence for the nitric oxide-induced cleavage of the FeMet80 bond in ferrous native cytochrome c, and allow estimation of the free energy associated to the heme-iron sixth coordination bond ( > 10 kJ mol-1, at 10°C).

Original languageEnglish
Pages (from-to)273-280
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume53
Issue number4
DOIs
Publication statusPublished - 1994

Fingerprint

Cytochromes c
Thermodynamics
Horses
Nitric Oxide
Derivatives
Paramagnetic resonance
Cytochromes a3
Armoracia
Cytochrome-c Peroxidase
Beef
Equilibrium constants
Electron Transport Complex IV
Heme
Yeast
Free energy
Saccharomyces cerevisiae
Absorption spectra
Spectrum Analysis
Iron
Display devices

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative : A spectroscopic and thermodynamic Study. / Ascenzi, Paolo; Coletta, Massimo; Santucci, Roberto; Polizio, Francesca; Desideri, Alessandro.

In: Journal of Inorganic Biochemistry, Vol. 53, No. 4, 1994, p. 273-280.

Research output: Contribution to journalArticle

Ascenzi, Paolo ; Coletta, Massimo ; Santucci, Roberto ; Polizio, Francesca ; Desideri, Alessandro. / Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative : A spectroscopic and thermodynamic Study. In: Journal of Inorganic Biochemistry. 1994 ; Vol. 53, No. 4. pp. 273-280.
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N2 - Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative has been investigated quantitatively by EPR and absorbance spectroscopy. The X-band EPR spectra and the absorption spectra in the Soret region of the nitrosylated derivative of ferrous native and carboxymethylated cytochrome c display the same basic characteristics reported for the beef heart cytochrome a3 in cytochrome c oxidase, and horseradish and baker's yeast cytochrome c peroxidase, as well as the high affinity form of oxygen carrying proteins. Values of the dissociation equilibrium constant for nitrosylation of ferrous native and carboxymethylated cytochrome c are 8.2 × 10-6 M and ≤ 5 × 10-8 M, respectively, at pH 7.0 and 10°C. The results here reported represent clearcut evidence for the nitric oxide-induced cleavage of the FeMet80 bond in ferrous native cytochrome c, and allow estimation of the free energy associated to the heme-iron sixth coordination bond ( > 10 kJ mol-1, at 10°C).

AB - Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative has been investigated quantitatively by EPR and absorbance spectroscopy. The X-band EPR spectra and the absorption spectra in the Soret region of the nitrosylated derivative of ferrous native and carboxymethylated cytochrome c display the same basic characteristics reported for the beef heart cytochrome a3 in cytochrome c oxidase, and horseradish and baker's yeast cytochrome c peroxidase, as well as the high affinity form of oxygen carrying proteins. Values of the dissociation equilibrium constant for nitrosylation of ferrous native and carboxymethylated cytochrome c are 8.2 × 10-6 M and ≤ 5 × 10-8 M, respectively, at pH 7.0 and 10°C. The results here reported represent clearcut evidence for the nitric oxide-induced cleavage of the FeMet80 bond in ferrous native cytochrome c, and allow estimation of the free energy associated to the heme-iron sixth coordination bond ( > 10 kJ mol-1, at 10°C).

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