scholarly journals N-Methyl Mesoporphyrin IX Inhibits Phycocyanin, but Not Chlorophyll Synthesis in Cyanidium caldarium

1983 ◽  
Vol 71 (2) ◽  
pp. 263-268 ◽  
Author(s):  
Samuel I. Beale ◽  
Nancy C. Chen
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.


Author(s):  
M. R. Edwards ◽  
J. D. Mainwaring

Although the general ultrastructure of Cyanidium caldarium, an acidophilic, thermophilic alga of questionable taxonomic rank, has been extensively studied (see review of literature in reference 1), some peculiar ultrastructural features of the chloroplast of this alga have not been noted by other investigators.Cells were collected and prepared for thin sections at the Yellowstone National Park and were also grown in laboratory cultures (45-52°C; pH 2-5). Fixation (glutaraldehyde-osmium), dehydration (ethanol), and embedding (Epon 812) were accomplished by standard methods. Replicas of frozenfracture d- etched cells were obtained in a Balzers apparatus. In addition, cells were examined after disruption in a French Press.


2019 ◽  
Vol 45 (3) ◽  
pp. 460 ◽  
Author(s):  
Ning HE ◽  
Xue-Yang WANG ◽  
Liang-Zi CAO ◽  
Da-Wei CAO ◽  
Yu LUO ◽  
...  

Crop Science ◽  
1979 ◽  
Vol 19 (2) ◽  
pp. 261-264 ◽  
Author(s):  
T. Gulya ◽  
J. M. Dunleavy

2000 ◽  
Vol 1456 (2-3) ◽  
pp. 99-107 ◽  
Author(s):  
Leslie E. Eisele ◽  
Sasha H. Bakhru ◽  
Xuemei Liu ◽  
Robert MacColl ◽  
Mercedes R. Edwards
Keyword(s):  

1980 ◽  
Vol 65 (3) ◽  
pp. 469-471 ◽  
Author(s):  
Richard J. Ellis ◽  
Charles Timson

2002 ◽  
Vol 362 (2) ◽  
pp. 423-432 ◽  
Author(s):  
Johanna E. CORNAH ◽  
Jennifer M. ROPER ◽  
Davinder Pal SINGH ◽  
Alison G. SMITH

Ferrochelatase is the terminal enzyme of haem biosynthesis, catalysing the insertion of ferrous iron into the macrocycle of protoporphyrin IX, the last common intermediate of haem and chlorophyll synthesis. Its activity has been reported in both plastids and mitochondria of higher plants, but the relative amounts of the enzyme in the two organelles are unknown. Ferrochelatase is difficult to assay since ferrous iron requires strict anaerobic conditions to prevent oxidation, and in photosynthetic tissues chlorophyll interferes with the quantification of the product. Accordingly, we developed a sensitive fluorimetric assay for ferrochelatase that employs Co2+ and deuteroporphyrin in place of the natural substrates, and measures the decrease in deuteroporphyrin fluorescence. A hexane-extraction step to remove chlorophyll is included for green tissue. The assay is linear over a range of chloroplast protein concentrations, with an average specific activity of 0.68nmol·min−1·mg of protein−1, the highest yet reported. The corresponding value for mitochondria is 0.19nmol·min−1·mg of protein−1. The enzyme is inhibited by N-methylprotoporphyrin, with an estimated IC50 value of ≈ 1nM. Using this assay we have quantified ferrochelatase activity in plastids and mitochondria from green pea leaves, etiolated pea leaves and pea roots to determine the relative amounts in the two organelles. We found that, in all three tissues, greater than 90% of the activity was associated with plastids, but ferrochelatase was reproducibly detected in mitochondria, at levels greater than the contaminating plastid marker enzyme, and was latent. Our results indicate that plastids are the major site of haem biosynthesis in higher plant cells, but that mitochondria also have the capacity for haem production.


Planta ◽  
1976 ◽  
Vol 132 (3) ◽  
pp. 291-295 ◽  
Author(s):  
H. Kasemir ◽  
G. Prelim

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