The presence of the low molecular mass carbonic anhydrase in photosystem II of C3 higher plants

2019 ◽  
Vol 232 ◽  
pp. 94-99 ◽  
Author(s):  
Lyudmila Ignatova ◽  
Elena Zhurikova ◽  
Boris Ivanov
Keyword(s):  
Photosystem Ii ◽  
Carbonic Anhydrase ◽  
Molecular Mass ◽  
Higher Plants

scholarly journals N-terminal sequencing of photosystem II low-molecular-mass proteins 5 and 4.1 kDa components of the O2 -evolving core complex from higher plants

FEBS Letters ◽  
1989 ◽  
Vol 242 (2) ◽  
pp. 263-269 ◽  
Author(s):  
Masahiko Ikeuchi ◽  
Koji Takio ◽  
Yorinao Inoue
Keyword(s):  
Photosystem Ii ◽  
Molecular Mass ◽  
Higher Plants ◽  
Core Complex

Photosystem II associated carbonic anhydrase activity in higher plants is situated in core complex

FEBS Letters ◽  
2004 ◽  
Vol 577 (1-2) ◽  
pp. 305-308 ◽  
Author(s):  
M.S. Khristin ◽  
L.K. Ignatova ◽  
N.N. Rudenko ◽  
B.N. Ivanov ◽  
V.V. Klimov
Keyword(s):  
Photosystem Ii ◽  
Carbonic Anhydrase ◽  
Higher Plants ◽  
Carbonic Anhydrase Activity ◽  
Core Complex

scholarly journals Carbonic Anhydrases in Photosynthesizing Cells of C3 Higher Plants

Metabolites ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 73 ◽  
Author(s):  
Lyudmila Ignatova ◽  
Natalia Rudenko ◽  
Elena Zhurikova ◽  
Maria Borisova-Mubarakshina ◽  
Boris Ivanov
Keyword(s):  
Plasma Membrane ◽  
Carbonic Anhydrase ◽  
Environmental Conditions ◽  
Organic Molecules ◽  
Higher Plants ◽  
C3 Plants ◽  
Coherent System ◽  
Carbonic Anhydrases ◽  
Chloroplast Stroma ◽  
Different Parts

The review presents data on the location, nature, properties, number, and expression of carbonic anhydrase genes in the photosynthesizing cells of C3 plants. The available data about the presence of carbonic anhydrases in plasma membrane, cytoplasm, mitochondria, chloroplast stroma and thylakoids are scrutinized. Special attention was paid to the presence of carbonic anhydrase activities in the different parts of thylakoids, and on collation of sources of these activities with enzymes encoded by the established genes of carbonic anhydrases. The data are presented to show that the consistent incorporation of carbonic anhydrases belonging to different families of these enzymes forms a coherent system of CO2 molecules transport from air to chloroplasts in photosynthesizing cells, where they are included in organic molecules in the carboxylation reaction. It is discussed that the manifestation of the activity of a certain carbonic anhydrase depends on environmental conditions and the stage of ontogenesis.

scholarly journals Crystal structure of the PsbQ protein of photosystem II from higher plants

EMBO Reports ◽  
2003 ◽  
Vol 4 (9) ◽  
pp. 900-905 ◽  
Author(s):  
Vito Calderone ◽  
Michela Trabucco ◽  
Andreja Vujičić ◽  
Roberto Battistutta ◽  
Giorgio Mario Giacometti ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Higher Plants

scholarly journals Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy

2021 ◽  
Vol 7 (9) ◽  
pp. 131
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
Yiannis Sanakis ◽  
George Mitrikas
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Spinacia Oleracea ◽  
Higher Plants ◽  
Correlation Spectroscopy ◽  
Oxygen Evolving Complex ◽  
Higher Plant ◽  
Proton Coupled Electron Transfer ◽  
S Oxidation

The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the oxygen evolving complex (OEC) of PSII. Two tyrosine residues D1-Tyr161 (YZ) and D2-Tyr160 (YD) are symmetrically placed in the two core subunits D1 and D2 and participate in proton coupled electron transfer reactions. YZ of PSII is near the OEC and mediates electron coupled proton transfer from Mn4Ca to the photooxidizable chlorophyll species P680+. YD does not directly interact with OEC, but is crucial for modulating the various S oxidation states of the OEC. In PSII from higher plants the environment of YD• radical has been extensively characterized only in spinach (Spinacia oleracea) Mn- depleted non functional PSII membranes. Here, we present a 2D-HYSCORE investigation in functional PSII of spinach to determine the electronic structure of YD• radical. The hyperfine couplings of the protons that interact with the YD• radical are determined and the relevant assignment is provided. A discussion on the similarities and differences between the present results and the results from studies performed in non functional PSII membranes from higher plants and PSII preparations from other organisms is given.

Isolation of Photosystem II-Enriched Membranes and the Oxygen-Evolving Complex Subunit Proteins From Higher Plants

2004 ◽  
pp. 029-036
Author(s):  
Yasusi Yamamoto ◽  
Shinsuke Sakuma ◽  
Jian-Ren Shen
Keyword(s):  
Photosystem Ii ◽  
Higher Plants ◽  
Oxygen Evolving Complex ◽  
Oxygen Evolving
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