scholarly journals Organisation of Photosystem I and Photosystem II in red alga Cyanidium caldarium: Encounter of cyanobacterial and higher plant concepts

2007 ◽  
Vol 1767 (6) ◽  
pp. 725-731 ◽  
Author(s):  
Zdenko Gardian ◽  
Ladislav Bumba ◽  
Adam Schrofel ◽  
Miroslava Herbstova ◽  
Jana Nebesarova ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Red Alga ◽  
Cyanidium Caldarium ◽  
Higher Plant

scholarly journals Stoichiometry of Photosystem I, Photosystem II, and Phycobilisomes in the Red Alga Porphyridium cruentum as a Function of Growth Irradiance

1989 ◽  
Vol 91 (3) ◽  
pp. 1179-1187 ◽  
Author(s):  
Francis X. Cunningham ◽  
Ronald J. Dennenberg ◽  
Laszlo Mustardy ◽  
Paul A. Jursinic ◽  
Elisabeth Gantt
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Red Alga ◽  
Porphyridium Cruentum ◽  
Growth Irradiance

scholarly journals Biochemical and structural analyses of a higher plant photosystem II supercomplex of a photosystem I-less mutant of barley

FEBS Journal ◽  
2006 ◽  
Vol 273 (20) ◽  
pp. 4616-4630 ◽  
Author(s):  
Tomas Morosinotto ◽  
Roberto Bassi ◽  
Sara Frigerio ◽  
Giovanni Finazzi ◽  
Edward Morris ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Higher Plant

scholarly journals Growth under Red Light Enhances Photosystem II Relative to Photosystem I and Phycobilisomes in the Red Alga Porphyridium cruentum

1990 ◽  
Vol 93 (3) ◽  
pp. 888-895 ◽  
Author(s):  
Francis X. Cunningham ◽  
Ronald J. Dennenberg ◽  
Paul A. Jursinic ◽  
Elisabeth Gantt
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Red Light ◽  
Red Alga ◽  
Porphyridium Cruentum

Cloning, Expression of the psbU Gene, and Functional Studies of the Recombinant 12-kDa Protein of Photosystem II from a Red Alga Cyanidium caldarium

1999 ◽  
Vol 260 (1) ◽  
pp. 245-250 ◽  
Author(s):  
Hisataka Ohta ◽  
Akinori Okumura ◽  
Satoshi Okuyama ◽  
Ai Akiyama ◽  
Masako Iwai ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Red Alga ◽  
Cyanidium Caldarium ◽  
Functional Studies

scholarly journals In Silico Analysis of Relationship between Proteins from Plastid Genome of Red Alga Palmaria sp. (Japan) and Angiotensin I Converting Enzyme Inhibitory Peptides

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 190 ◽  
Author(s):  
Yuya Kumagai ◽  
Yoshikatsu Miyabe ◽  
Tomoyuki Takeda ◽  
Kohsuke Adachi ◽  
Hajime Yasui ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Plastid Genome ◽  
Red Alga ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Plastid proteins are one of the main components in red algae. In order to clarify the angiotensin I converting enzyme (ACE) inhibitory peptides from red alga Palmaria sp. (Japan), we determined the plastid genome sequence. The genome possesses 205 protein coding genes, which were classified as genetic systems, ribosomal proteins, photosystems, adenosine triphosphate (ATP) synthesis, metabolism, transport, or unknown. After comparing ACE inhibitory peptides between protein sequences and a database, photosystems (177 ACE inhibitory peptides) were found to be the major source of ACE inhibitory peptides (total of 751). Photosystems consist of phycobilisomes, photosystem I, photosystem II, cytochrome complex, and a redox system. Among them, photosystem I (53) and II (51) were the major source of ACE inhibitory peptides. We found that the amino acid sequence of apcE (14) in phycobilisomes, psaA (18) and psaB (13) in photosystem I, and psbB (11) and psbC (10) in photosystem II covered a majority of bioactive peptide sequences. These results are useful for evaluating the bioactive peptides from red algae.

scholarly journals Unique organization of photosystem I–light-harvesting supercomplex revealed by cryo-EM from a red alga

2018 ◽  
Vol 115 (17) ◽  
pp. 4423-4428 ◽  
Author(s):  
Xiong Pi ◽  
Lirong Tian ◽  
Huai-En Dai ◽  
Xiaochun Qin ◽  
Lingpeng Cheng ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Photosystem I ◽  
Light Harvesting ◽  
Higher Plants ◽  
Red Alga ◽  
Cyanidioschyzon Merolae ◽  
Higher Plant ◽  
Light Harvesting Complex ◽  
Red Algal ◽  
Eukaryotic Organisms

Photosystem I (PSI) is one of the two photosystems present in oxygenic photosynthetic organisms and functions to harvest and convert light energy into chemical energy in photosynthesis. In eukaryotic algae and higher plants, PSI consists of a core surrounded by variable species and numbers of light-harvesting complex (LHC)I proteins, forming a PSI-LHCI supercomplex. Here, we report cryo-EM structures of PSI-LHCR from the red alga Cyanidioschyzon merolae in two forms, one with three Lhcr subunits attached to the side, similar to that of higher plants, and the other with two additional Lhcr subunits attached to the opposite side, indicating an ancient form of PSI-LHCI. Furthermore, the red algal PSI core showed features of both cyanobacterial and higher plant PSI, suggesting an intermediate type during evolution from prokaryotes to eukaryotes. The structure of PsaO, existing in eukaryotic organisms, was identified in the PSI core and binds three chlorophylls a and may be important in harvesting energy and in mediating energy transfer from LHCII to the PSI core under state-2 conditions. Individual attaching sites of LHCRs with the core subunits were identified, and each Lhcr was found to contain 11 to 13 chlorophylls a and 5 zeaxanthins, which are apparently different from those of LHCs in plant PSI-LHCI. Together, our results reveal unique energy transfer pathways different from those of higher plant PSI-LHCI, its adaptation to the changing environment, and the possible changes of PSI-LHCI during evolution from prokaryotes to eukaryotes.

Purification And Crystallization Of Photosystem Ii Dimer Complex From A Red Alga Cyanidium Caldarium

2008 ◽  
pp. 353-356
Author(s):  
Hideyuki Adachi ◽  
Isao Enami ◽  
Takahiro Henmi ◽  
Nobuo Kamiya ◽  
Jian-Ren Shen
Keyword(s):  
Photosystem Ii ◽  
Red Alga ◽  
Cyanidium Caldarium
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