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Author Dyson, H.J.; Beattie, J.K. openurl 
  Title Spin state and unfolding equilibria of ferricytochrome c in acidic solutions Type Journal Article
  Year 1982 Publication The Journal of Biological Chemistry Abbreviated Journal J Biol Chem  
  Volume 257 Issue 5 Pages 2267-2273  
  Keywords Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature  
  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.  
  Address  
  Corporate Author Thesis  
  Publisher Place of Publication Editor  
  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 0021-9258 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:6277891 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3807  
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Author Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. openurl 
  Title Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements Type Journal Article
  Year 1989 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta  
  Volume 996 Issue 1-2 Pages 49-56  
  Keywords Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Methemoglobin/*ultrastructure; Motion; Protein Conformation; Temperature; Thermodynamics; Water  
  Abstract Temperature-dependent EPR and temperature-jump measurements have been carried out, in order to examine the high-spin to low-spin transition of aquomethemogobin (pH 6.0). Relaxation rates and equilibrium constants could be determined as a function of temperature. As a reaction mechanism for the high-spin to low-spin transition, the binding of N epsilon of His E7 to the heme iron had been proposed; the same mechanism had been suggested for the ms-effect, found in temperature-jump experiments on aquomethemoglobin. A comparison of the thermodynamic quantities, deduced form the measurements in this paper, gives evidence that indeed the same reaction is investigated in both cases. Our results and most of the findings of earlier studies on the spin-state transitions of aquomethemoglobin, using susceptibility, optical, or EPR measurements, can be explained by the transition of methemoglobin with H2O as ligand (with high-spin state at all temperatures) and methemoglobin with ligand N epsilon of His E7 (with a low-spin ground state). Thermal fluctuations of large amplitude have to be postulated for the reaction to take place, so this reaction may be understood as a probe for the study of protein dynamics.  
  Address Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G  
  Corporate Author Thesis  
  Publisher Place of Publication Editor  
  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition  
  ISSN 0006-3002 ISBN Medium  
  Area Expedition Conference  
  Notes PMID:2544230 Approved no  
  Call Number Equine Behaviour @ team @ Serial 3803  
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