Affinity and activity of non-native quinones at the Q(B) site of bacterial photosynthetic reaction centers.

ABSTRACT: Purple, photosynthetic reaction centers from Rhodobacter sphaeroides bacteria use ubiquinone (UQ10) as both primary (Q(A)) and secondary (Q(B)) electron acceptors. Many quinones reconstitute Q(A) function, while a few will act as Q(B). Nine quinones were tested for their ability to bind and reconstitute Q(A) and Q(B) functions. Only ubiquinone (UQ) reconstitutes both functions in the same protein. The affinities of the non-native quinones for the Q(B) site were determined by a competitive inhibition assay. The affinities of benzoquinones, naphthoquinone (NQ), and 2-methyl-NQ for the Q(B) site are 7 ± 3 times weaker than that at Q(A) site. However, di-ortho-substituted NQs and anthraquinone bind tightly to the Q(A) site (K d ≤ 200 nM), and ≥1,000 times more weakly to the Q(B) site, perhaps

SUBMITTER: Zhang X 

PROVIDER: S-EPMC4442677 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature