Porphyrin-proteinoid complexes as models of prebiotic photosensitizers.
Photochemical activity as well as some spectral properties of various porphyrins and their model complexes with proteinoids were studied. Photochemical activity increased from the less advanced biosynthetic chlorophyll precursors to the more advanced compounds. The significant increase was detected as a result of the formation of complexes of phytol-containing porphyrins with proteinoids, which brings about the disaggregation of the pigment clusters formed in the aqueous environment. Hemin is photochemically inactive, either alone or in complex with proteinoid. Although hemoproteinoid was demonstrated to be able to catalyse photochemical electron transfer, its activity is about 20 times lower when compared with the chlorophyll a-proteinoid complex. Experimental results are discussed in context of the early evolution of photosynthesis.
Masinovský
Z
Z
Laboratory of Evolutionary Biology, Czechoslovak Academy of Sciences, Prague.
Lozovaya
G I
GI
Sivash
A A
AA
Drasner
M
M
D002734:Chlorophyll; D002735:Chlorophyllides; D006427:Hemin; D008954:Models, Biological; D010674:Pheophytins; D010777:Photochemistry; D011166:Porphyrins; D011524:Protoporphyrins; D013054:Spectrophotometry, Atomic; D013057:Spectrum Analysis; D014578:Uroporphyrins
D002735:Chlorophyllides; D010674:Pheophytins; D011166:Porphyrins; D011524:Protoporphyrins; D014578:Uroporphyrins; D002734:Chlorophyll; D006427:Hemin; C049692:tetraphenylporphine