Temperature dependence of cytochrome photooxidation and conformational dynamics of Chromatium reaction center complexes.

A temperature dependence of multiheme cytochrome c oxidation induced by a laser pulse was studied in photosynthetic reaction center preparations from Chromatium minutissimum. Absorbance changes and kinetic characteristics of the reaction were measured under redox conditions where one or all of the hemes of the cytochrome subunit are chemically reduced (E h =+300 mV or E h =-20 to -60 mV respectively). In the first case photooxidation is inhibited at temperatures lower than 190-200 K with the rate constant of the photooxidation reaction being practically independent on temperature over the range of 300 to 190 K (k=2.2×10(5) s(-1)). Under reductive conditions (E h =-20 to -60 mV) lowering the temperature to 190-200 K causes the reaction to slow from k=8.3×10(5) s(-1) to 2.1×10(4) s(-1). Under further cooling down to the liquid nitrogen temperature, the reaction rate changes negligibly. The absorption amplitude decreases by 30-40% on lowering the temperature. A new physical mechanism of the observed critical effects of temperature on the rate and absorption amplitude of the multiheme cytochrome c oxidation reaction is proposed. The mechanism suggests a close interrelation between conformational mobility of the protein and elementary electron tunneling act. The effect of "freezing" conformational motion is described in terms of a local diffusion along a random rough potential.