Analysis of absorption spectra changes induced by temperature lowering on phycobilisomes, thylakoids and chlorophyll-protein complexes.
Using fourth derivative analysis, differences between room and low temperature absorption spectra were studied. The positions of most absorption bands of the water-soluble, accessory pigment complex, the phycobilisome, remained unchanged after cooling. The stability of the wavelength positions of chlorophyll a forms in vivo as a function of temperature (Gulyaev, B.A. and Litvin, F.F. (1967) Biofizika 12, 845--854) was generally confirmed. The wavelength positions of all chlorophyll a forms in the P-700 chlorophyll a protein complex were unchanged when the preparations were cooled to -196 degrees C. Likewise, with other chlorophyll-containing materials: the light-harvesting chlorophyll a/b protein complex and the thylakoids of higher plants, algae, and cyanobacteria, the wavelengths positions of most chlorophyll a forms were stable upon cooling. An exception was a 680 nm chlorophyll a band which was generally split at low temperature into two bands with the materials investigated. An interpretation of the multiplicity of chlorophyll spectral forms and the spectral changes induced by cooling for these forms is given using exciton theory and the energy-coupling variation of chlorophyll a molecules.
D002734:Chlorophyll / Q000378:metabolism*; D000460:Chlorophyta / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D000458:Cyanobacteria / Q000378:metabolism; D010788:Photosynthesis; D045524:Phycobilisomes; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism; D013045:Species Specificity; D013053:Spectrophotometry; D013696:Temperature
D045524:Phycobilisomes; D010940:Plant Proteins; D002734:Chlorophyll