The Conformational Flexibility of Oxidized Cytochrome c Studied through Its Interaction with NH3 and at High Temperatures

  • Banci L
  • Bertini I
  • Spyroulias G
 et al. 
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The binding of ammonia to oxidized horse heart cytochrome c has been studied by 1H-NMR, EPR, and CD spectroscopy at pH = 8.0. The affinity constant of the ligand is in the range 1.5−4 M−1. The 1H-NMR spectra of the heme group have been found to be similar to those of the high-pH forms, high-temperature forms, and cyanide adduct of the Met80Ala mutant of S. cerevisiae iso-1-cytochrome c. The assignment of a number of signals has led to the determination of the values of the magnetic anisotropy and of the orientation of its axes. The latter are similar to those of the Met80Ala cyanide derivative. The assignment of the high-temperature species has been further pursued during this research. The analysis of the NMR data of the NH3 adduct leads to the conclusion that substitution of Met80 at high pH or high temperature occurs through a ligand with cylindrical symmetry. This supports the suggestion that Met80 is substituted by a lysine at high pH.

Author-supplied keywords

  • 0
  • 8
  • and cd spectroscopy
  • at ph
  • by 1 h-nmr
  • c has been studied
  • cytochrome
  • cytochrome c
  • epr
  • heme proteins
  • hyperfine shift
  • magnetic susceptibility anisotropy
  • nmr spectroscopy
  • the affinity constant of
  • the binding of ammonia
  • the ligand is in
  • the range
  • to oxidized horse heart

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  • Lucia Banci

  • Ivano Bertini

  • Georgios A Spyroulias

  • Paola Turano

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