: Nature 1993 Dec 9;366(6455):517-8

Atavistic Reaction Centre

Coleman W. J. , Youvan D. C.

Evolutionary models of the photosynthetic reaction centre in the purple bacteria propose that an an ancestral protein (a putative homodimer, X2 ) may have had two parallel electron transfer pathways, each of them capable of reducing a quinone molecule.   Over time, the two identical sequences are thought to have diverged and created a heterodimeric structure, wherein the two quinone binding sites became more specialized and the two quinones (QA and QB) accepted electrons in series.   The recent discovery of apparently homodimeric reaction-centre complexes in the non-purple bacteria Heliobacillus mobilis and Chlorobium limicola, combined with the fact that the two quinones in some of the purple bacteria are chemically identical but nevertheless functionally different,  raises the possibility that evolutionary selection for more efficient electron transfer led to a sequence divergence within the purple bacterial reaction centre; eventually forming the heterodimeric L- and M-subunit core complex. 

           

 

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