P. Mathis et al., INTERACTION BETWEEN CYTOCHROME-C AND THE PHOTOSYNTHETIC REACTION-CENTER OF PURPLE BACTERIA - BEHAVIOR AT LOW-TEMPERATURE, Biochimie, 76(6), 1994, pp. 569-579
In purple photosynthetic bacteria the electron donor to the special pa
ir, after its oxidation by a light-induced reaction, is a c-type cytoc
hrome: either a soluble monoheme cytochrome which forms a transitory c
omplex with the reaction center, or a tetraheme cytochrome which remai
ns permanently bound to the reaction center. The effects of low temper
atures on electron transfer in the complex are presented and discussed
. They provide estimates for the reorganization energy. The most promi
nent effect of low temperature is that a dominant fast phase of electr
on transfer becomes impossible at a temperature of around 250 K (monoh
eme cytochrome) or located between 250 K and 80 K according to the red
ox state (tetraheme cytochrome). This inhibition is attributed to a fr
eezing-like transition of pools of water molecules which blocks struct
ural changes of the protein which are normally associated with the cyt
ochrome oxidation.