I. Agalidis et P. Sebban, ENERGETICS OF THE QUINONE ELECTRON-ACCEPTOR COMPLEX IN RUBRIVIVAX-GELATINOSUS, Biochimica et biophysica acta. Bioenergetics, 1232(3), 1995, pp. 180-186
The pH and temperature dependences of the free energy stabilization of
the Q(A)(-) and Q(B)(-) semiquinone anions (Q(A) and Q(B) are respect
ively the primary and secondary quinone electron accepters) were studi
ed in antenna-reaction centre complex from Rubrivivax(R.) gelatinosus.
This was achieved by measuring the rate constants of the P(+)Q(A)(-),
(k(AP)) and P(+)Q(B)(-) (k(BP)) (P is the primary electron donor) cha
rge recombination processes by flash-induced absorption spectroscopy.
Despite the high primary sequence analogies of the Q(A) and Q(B) prote
in pockets between R. gelatinosus and the much more studied species as
Rps. viridis, Rb. sphaeroides and Rb. capsulatus, the energetic behav
iour of the quinone complex of R. gelatinosus appears to be somewhat d
ifferent: (i) above pH 10, k(AP) decreases, whereas it increases in Rp
s. viridis; this suggests the presence of a protonatable group that st
abilizes I- (I is a bacteriopheophytin electron acceptor) rather than
Q(A)(-); (ii) the pH dependence of k(BP) is unusually flat in the rang
e 4-7.5, possibly reflecting that a substantial part of the P(+)Q(B)(-
), charge recombination proceeds via the direct route through the prot
ein by an electron tunnelling mechanism, at variance to what is observ
ed in the three species mentioned above; (iii) the very substantial in
crease of k(BP) observed above pH 7.5 is reasonably well described by
the presence of two apparent protonatable groups: PK1QB = 9.4, pK(1QB-
),= 11 and pK(2QB) = 8.5, pK(2QB-) = 9.4. The latter group was not rep
orted in Rps. viridis, Rb. sphaeroides or Rb. capsulatus. We conclude
that the apparent pK values measured here in R. gelatinosus may reflec
t the contribution as a whole of several and/or distant groups rather
than of well-defined residues.