A reduced model of the fluorescence from the cyanobacterial photosynthetic apparatus designed for the in situ detection of cyanobacteria.
Fluorometric determination of the chlorophyll (Chl) content of cyanobacteria is impeded by the unique structure of their photosynthetic apparatus, i.e., the phycobilisomes (PBSs) in the light-harvesting antennae. The problems are caused by the variations in the ratio of the pigment PC to Chl a resulting from adaptation to varying environmental conditions. In order to include cyanobacteria in fluorometric analysis of algae, a simplified energy distribution model describing energy pathways in the cyanobacterial photosynthetic apparatus was conceptualized. Two sets of mathematical equations were derived from this model and tested. Fluorescence of cyanobacteria was measured with a new fluorometer at seven excitation wavelength ranges and at three detection channels (650, 685 and 720 nm) in vivo. By employing a new fit procedure, we were able to correct for variations in the cyanobacterial fluorescence excitation spectra and to account for other phytoplankton signals. The effect of energy-state transitions on the PC fluorescence emission of PBSs was documented. The additional use of the PC fluorescence signal in combination with our recently developed mathematical approach for phytoplankton analysis based on Chl fluorescence spectroscopy allows a more detailed study of cyanobacteria and other phytoplankton in vivo and in situ.
Beutler
M
M
Max-Planck-Institut (MPI) für Limnologie, Plön, Germany. MartinBeutler@gmx.de
Wiltshire
K H
KH
Arp
M
M
Kruse
J
J
Reineke
C
C
Moldaenke
C
C
Hansen
U-P
UP
D000458:Cyanobacteria / Q000302:isolation & purification / Q000378:metabolism*; D005453:Fluorescence; D008954:Models, Biological; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045524:Phycobilisomes
D045322:Photosynthetic Reaction Center Complex Proteins; D045524:Phycobilisomes