Laser flash-induced photoreduction of photosynthetic ferredoxins and flavodoxin by 5-deazariboflavin and by a viologen analogue.

Laser flash photolysis has been used to compare the kinetics of reduction of ferredoxin isoforms from the green alga Monoraphidium braunii, and the ferredoxin and flavodoxin from the cyanobacterium Anabaena PCC 7119, by 5-deazariboflavin semiquinone (dRfH.) and the viologen analogue 1,1'-propylene-2,2'-bipyridyl (PDQ.+). Similar ionic strength-independent second-order rate constants (1.4 x 10(8) M-1 s-1) were obtained for the reduction of both algal ferredoxin isoforms by dRfH.. For the reduction of oxidized flavodoxin by dRfH., a more complex behavior was observed, with a second-order rate constant for dRfH. decay of 1.8 x 10(8) M-1 s-1, and a first-order (i.e. protein concentration independent) rate constant of 450 s-1, that probably corresponds to the protonation of the FMN semiquinone cofactor, which occurs subsequent to electron transfer. A value of 5 x 10(7) M-1 s-1 was obtained for the second-order rate constant of flavodoxin semiquinone reduction by dRfH.. The reduction of ferredoxins and flavodoxin semiquinone by PDQ.+ showed nonlinear protein concentration dependencies, consistent with a minimal two-step mechanism involving complex formation followed by intracomplex electron transfer. A negative ionic strength effect on the kinetic constants was obtained, indicating the existence of attractive electrostatic interactions during electron transfer. With all the ferredoxins the k infinity values (rate constants extrapolated to infinite ionic strength) for the second-order step of the reduction process (complex formation) are smaller than previously reported for spinach ferredoxin, although Anabaena ferredoxin is somewhat more reactive than are the algal ferredoxins with the viologen.(ABSTRACT TRUNCATED AT 250 WORDS)