Cryptophyte algae
are well-known for their ability to survive under
low light conditions using their auxiliary light harvesting antennas,
phycobiliproteins. Mainly acting to absorb light where chlorophyll
cannot (500–650 nm), phycobiliproteins also play an instrumental
role in helping cryptophyte algae respond to changes in light intensity
through the process of photoacclimation. Until recently, photoacclimation
in cryptophyte algae was only observed as a change in the cellular
concentration of phycobiliproteins; however, an additional photoacclimation
response was recently discovered that causes shifts in the phycobiliprotein
absorbance peaks following growth under red, blue, or green light.
Here, we reproduce this newly identified photoacclimation response
in two species of cryptophyte algae and elucidate the origin of the
response on the protein level. We compare isolated native and photoacclimated
phycobiliproteins for these two species using spectroscopy and mass
spectrometry, and we report the X-ray structures of each phycobiliprotein
and the corresponding photoacclimated complex. We find that neither
the protein sequences nor the protein structures are modified by photoacclimation.
We conclude that cryptophyte algae change one chromophore in the phycobiliprotein
β subunits in response to changes in the spectral quality of
light. Ultrafast pump–probe spectroscopy shows that the energy
transfer is weakly affected by photoacclimation