Oral Presentation The 42nd Lorne Conference on Protein Structure and Function 2017

Evolution of light harvesting proteins:  Single residue insertion switches the quaternary structure and exciton states in cryptophyte phycobiliproteins (#12)

Stephen Harrop 1 , Krystyna Wilk 1 , Alistair Laos 1 , Chang Ying Teng 2 , Beverley Green 2 , Kerstin Hoef-Emden 3 , Roger Hiller 4 , Pall Thordarson 1 , Gregory Scholes 5 , Paul Curmi 1
  1. University of New South Wales, Sydney, NSW, Australia
  2. University of British Columbia, Vancouver, Canada
  3. University of Cologne, Cologne, Germany
  4. Macquarie University, Sydney, Australia
  5. Princeton University, Princeton, USA

Are we at the dawn of quantum biology? The observation of coherent oscillations in the two-dimensional electronic spectra (2D ES) of photosynthetic proteins has led researchers to ask whether non-trivial quantum phenomena are biologically significant.  Coherent oscillations have been reported for the soluble light harvesting phycobiliprotein (PBP) antenna isolated from cryptophyte algae.  To probe the link between spectral properties and protein structure, we determined crystal structures of seven PBP light harvesting complexes isolated from different species. Each PBP is a dimer of αβ subunits where the structure of the αβ monomer is conserved, however, we discovered two dramatically distinct quaternary conformations, one that is specific to the genus Hemiselmis. Owing to steric effects emerging from a single amino acid insertion, the two αβ monomers are rotated by ~73° to an “open” configuration in contrast to the “closed” configuration of other cryptophyte PBPs. This structural change is significant for the light harvesting function because it disrupts the strong excitonic coupling between two central chromophores. 2D ES show marked cross-peak oscillations assigned to electronic and vibrational coherences in the case of the closed form. However, such features appear reduced, or absent, for open structures. Therefore cryptophytes have evolved a structural switch controlled by an amino acid insertion to modulate excitonic interactions and hence light harvesting. Transcriptomic studies of Hemiselmis species show that they carry and express genes for both open and closed form PBPs, indicating that the type of protein expressed (open or closed) is under the control of the organism. Thus, Hemiselmis algae appear to be able to switch between proteins that do and do not support non-trivial quantum phenomena. The real question is: do these quantum effects have biological value or are they just spandrels?