Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein

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Abstract

NMR and visible spectroscopy coupled to redox measurements were used to determine the equilibrium thermodynamic properties of the four haems in cytochrome c3, under conditions in which the protein was bound to ligands, the small anion phosphate and the protein rubredoxin with the iron in the active site replaced by zinc. Comparison of these results with data for the isolated cytochrome shows that binding of ligands causes only small changes in the reduction potentials of the haems and their pairwise interactions, and also that the redox-sensitive acid-base centre responsible for the redox-Bohr effect is essentially unaffected. Although neither of the ligands tested is a physiological partner of cytochrome c3, the small changes observed for the thermodynamic properties of cytochrome c3 bound to these ligands vs. the unbound state, indicate that the thermodynamic properties measured for the isolated protein are relevant for a physiological interpretation of the role of this cytochrome in the bioenergetic metabolism of Desulfovibrio.

Original languageEnglish
Pages (from-to)2251-2260
Number of pages10
JournalFebs Journal
Volume272
Issue number9
DOIs
Publication statusPublished - 1 May 2005

Keywords

  • Cytochrome c
  • Electron transfer
  • NMR
  • Protein docking
  • Thermodynamic properties

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