The EPR spectra of cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodopseudomonas sphaeroides were measured at liquid helium temperature. The purified cytochrome b-562 gives a high spin signal at g=6.0. Anaerobic titration of this signal confirmed the presence of two redox components with Em=40 and -110 mV at pH 7.5. These values are consistent with the published ones, Em= 55 and -100 mV at pH 7.0, that were optically estimated for the same type of preparation (Iba et al. (1985) FEBS Lett. 183, 151-154). The power saturation behavior of the g= 6.0 signal at different redox potentials indicated a direct spin-spin interaction between these two redox centers.
|Number of pages||4|
|Journal||Journal of biochemistry|
|Publication status||Published - Oct 1 1986|
All Science Journal Classification (ASJC) codes
- Molecular Biology