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Spin state and unfolding equilibria of ferricytochrome c in acidic solutions

Academic Article
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Overview

authors

  • Dyson, Jane
  • Beattie, J. K.

publication date

  • 1982

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions.

subject areas

  • Animals
  • Cytochrome c Group
  • Electron Spin Resonance Spectroscopy
  • Heme
  • Horses
  • Hydrogen-Ion Concentration
  • Kinetics
  • Ligands
  • Myocardium
  • Protein Binding
  • Protein Conformation
  • Spectrophotometry
  • Temperature
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 6277891
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Additional Document Info

start page

  • 2267

end page

  • 2273

volume

  • 257

issue

  • 5

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