The Temperature Dependence of the Electron Paramagnetic Resonance Spectrum of Ferricytochrome c Solutions Between 4.2 °K and 77 °K

1971 ◽  
Vol 49 (6) ◽  
pp. 695-699 ◽  
Author(s):  
C. Mailer ◽  
C. P. S. Taylor

Electron paramagnetic resonance (E.P.R.) signals from tuna ferricytochrome c solutions were obtained in the temperature range 4.2–77 °K. The microwave power and temperature dependence of the spectra obtained fit the theory for a Kramer's doublet split by a magnetic field. The g-values obtained are 1.25, 2.24, and 3.05 in agreement with other workers (Salmeen, I., and Palmer, G.: J. Chem. Phys. 48, 2049 (1968)). The g = 3.05 line changes from 380 G wide at 20–40 °K with Gaussian shape to 700 G wide at 77 °K with Lorentzian shape. Analysis shows that the Gaussian shape can be explained by variation in the rhombic symmetry of the heme iron environment, a ± 6% spread in rhombic potential being required to give a 380 G line width. At higher temperatures the line appears to be determined by the electron spin-lattice relaxation time. Below 20 °K the E.P.R. absorption signal is saturated, and a large E.P.R. dispersion signal appears, due to fast passage effects, which can be used to give further information on electron spin relaxation times.


1973 ◽  
Vol 51 (4) ◽  
pp. 472-475 ◽  
Author(s):  
R. A. Morton

The heme-associated, pH-induced transition in iodinated ferricytochrome c has been studied by electron paramagnetic resonance (E.P.R.) and absorption spectroscopy. The conversion from type III to type IV (as defined by Theorell, H., and Åkesson, Å.: J. Am. Chem. Soc. 63, 1812 (1941)) ferricytochrome c forms was dramatically altered by iodination of tyrosyl residues. Both absorption and E.P.R. spectra suggested that a transition between similar heme-iron coordination structures occurred with a pK of about 6 as compared with about 9 for native ferricytochrome c. At pH 4.4 the E.P.R. spectrum (liquid nitrogen temperature) of a frozen solution of iodinated ferricytochrome c was similar to the native type III at pH 7, except for an increased g = 6.0 signal from high-spin heme iron. At neutral pH the E.P.R. spectrum of the iodinated derivative was similar to type IV ferricytochrome c. The results give further support to the hypothesis that the pK of tyrosine 67 plays an important role in determining the pK of the III to IV transition.



Biochemistry ◽  
1997 ◽  
Vol 36 (31) ◽  
pp. 9446-9452 ◽  
Author(s):  
Yiannis Deligiannakis ◽  
Alain Boussac ◽  
Hervé Bottin ◽  
Véronique Perrier ◽  
Octavian Bârzu ◽  
...  


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