scholarly journals Biosynthesis of phycobiliproteins. Incorporation of biliverdin into phycocyanin of the red alga Cyanidium caldarium

1984 ◽  
Vol 219 (3) ◽  
pp. 905-909 ◽  
Author(s):  
S B Brown ◽  
J A Holroyd ◽  
D I Vernon

14C-labelled biliverdin IX alpha was administered to cultures of Cyanidium caldarium that were actively synthesizing photosynthetic pigments in the light. Between 9 and 12% of the phycobiliprotein chromophore produced in such cultures was derived from exogenous biliverdin. These results demonstrate that biliverdin is an intermediate in the biosynthesis of phycobiliproteins.

1989 ◽  
Vol 261 (1) ◽  
pp. 259-263 ◽  
Author(s):  
S B Brown ◽  
J A Holroyd ◽  
D I Vernon ◽  
Y K Shim ◽  
K M Smith

The later stages in the pathway of biosynthesis of phycocyanobilin, the chromophore of phycocyanin, were studied by using radiolabelled intermediates. Three possible pathways from biliverdin IX-alpha to phycocyanobilin were considered. 14C-labelled samples of key intermediates in two of the pathways, 3-vinyl-18-ethyl biliverdin IX-alpha and 3-ethyl-18-vinyl biliverdin IX-alpha, were synthesized chemically and were administered to cultures of Cyanidium caldarium that were actively synthesizing photosynthetic pigments in the light. Neither of these two compounds was apparently incorporated into the phycobiliprotein chromophore, suggesting that two of the three pathways were not operative. By elimination, the results imply that the third possible pathway, which involves phytochromobilin, the chromophore of phytochrome, represents the route for biosynthesis of phycocyanobilin. Unfortunately, since 14C-labelled phytochromobilin is not available, no direct proof of this pathway could be obtained. However, if correct, the present interpretation represents a unified pathway for biosynthesis of all plant bilins, via the intermediacy of phytochromobilin.


1982 ◽  
Vol 37 (11-12) ◽  
pp. 1057-1063 ◽  
Author(s):  
Hans-Peter Köst ◽  
Eva Benedikt

Abstract Dark-grown cells of the unicellular rhodophyte Cyanidium caldarium were incubated with 17 mmol/l 5-aminolevulinic acid in the dark. The excreted pigments were extracted with chloroform and butanol. The presence of biliverdin IX α in the chloroform-extract (besides phycocyanobilin and other pigments) was demonstrated using TLC, HPLC and chromic acid degradation. A pathway leading to phycocyanobilin is discussed. A green pigment from egg shells of Turdus merula (black bird) was also identified as biliverdin IX α with small amounts of protoporphyrin IX, using the same methods as above.


1987 ◽  
Vol 105 (2) ◽  
pp. 247-254 ◽  
Author(s):  
VITTORIA MARTINO RIGANO ◽  
VINCENZA VONA ◽  
CATELLO MARTINO ◽  
CARMELO RIGANO

1988 ◽  
Vol 254 (3) ◽  
pp. 907-910 ◽  
Author(s):  
J D Houghton ◽  
L Turner ◽  
S B Brown

Pigment synthesis in four strains of the unicellular red alga Cyanidium caldarium with different pigment-synthesizing patterns was inhibited in the presence of gabaculine (3-amino-2,3-dihydrobenzoic acid). Parallel inhibition of light-induced chlorophyll and phycocyanin synthesis was observed in strain III-D-2, which only synthesizes pigments in the light. Similar parallel inhibition was observed in the dark in mutant CPD, which is able to synthesize chlorophyll and phycocyanin in the absence of light. Inhibition of pigment synthesis in all strains was overcome by addition of 5-aminolaevulinic acid. Inhibition of phycocyanin synthesis in mutant GGB (unable to synthesize chlorophyll) and inhibition of chlorophyll synthesis in mutant III-C (unable to synthesize phycocyanin) were also observed. Gabaculine also inhibited the heterotrophic growth of C. caldarium in the dark. However, inhibition was overcome after an extended lag period, following which cell growth proceeded at a similar rate to that of control cells not exposed to gabaculine. Heterotrophic growth in cells pre-exposed to gabaculine was not inhibited by subsequent exposure. Possible mechanisms for this adaptation are discussed.


1984 ◽  
Vol 220 (3) ◽  
pp. 861-863 ◽  
Author(s):  
S B Brown ◽  
J A Holroyd ◽  
D I Vernon ◽  
O T G Jones

Dark-grown cells of the photosynthetic alga Cyanidium caldarium were shown to contain ferrochelatase activity, which increased markedly when the cells were induced to form pigments by exposure to light. Km values for the crude enzyme preparation were 14.8 microM and 6.5 microM for binding of Co2+ and deuteroporphyrin IX respectively.


1994 ◽  
Vol 26 (2) ◽  
pp. 136-138 ◽  
Author(s):  
Niji Ohta ◽  
Shigeyuki Kawano ◽  
Tsuneyoshi Kuroiwa

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