Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center

Biochemistry ◽  
1993 ◽  
Vol 32 (49) ◽  
pp. 13742-13748 ◽  
Author(s):  
Xiao Song Tang ◽  
Dexter A. Chisholm ◽  
G. Charles Dismukes ◽  
Gary W. Brudvig ◽  
Bruce A. Diner
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Spectroscopic Evidence ◽  
Synechocystis Pcc6803 ◽  
Close Interaction ◽  
Redox Active

scholarly journals A difference Fourier-transform infrared study of two redox-active tyrosine residues in photosystem II

1993 ◽  
Vol 90 (23) ◽  
pp. 11024-11028 ◽  
Author(s):  
G M MacDonald ◽  
K A Bixby ◽  
B A Barry
Keyword(s):  
Fourier Transform ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Fourier Transform Infrared ◽  
Active Species ◽  
Structural Factors ◽  
Infrared Study ◽  
Tyrosine Residues ◽  
Redox Active ◽  
Difference Fourier

Photosystem II, the photosynthetic water-oxidizing complex, contains two redox-active tyrosine residues. Although current models suggest that these tyrosines are located in symmetric positions in the reaction center, there are functional differences between them. To elucidate those structural factors that give rise to this functional asymmetry, we have used difference Fourier-transform infrared spectroscopy to obtain the vibrational difference spectrum associated with the oxidation of each of these redox-active residues. Isotopic labeling was employed to definitively assign vibrational lines to the redox-active tyrosines. This work has shown that the vibrational spectra of the two redox-active species are significantly different from each other. This result suggests that the structure of the redox-active residue helps to determine its role in electron transfer in the reaction center.

scholarly journals High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Koji Kato ◽  
Naoyuki Miyazaki ◽  
Tasuku Hamaguchi ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Physiological State ◽  
High Dose ◽  
Final State ◽  
X Ray ◽  
Redox States ◽  
X Ray Crystallography ◽  
Cryo Electron Microscopy ◽  
Redox Active ◽  
Beam Damage

AbstractPhotosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.

Excitonic States in Photosystem II Reaction Center

2005 ◽  
Vol 109 (48) ◽  
pp. 23051-23060 ◽  
Author(s):  
Nikolaj Ivashin ◽  
Sven Larsson
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Excitonic States

Characterization of bonding interactions of the intermediary electron acceptor in the reaction center of Photosystem II by FTIR spectroscopy

1990 ◽  
Vol 1016 (1) ◽  
pp. 49-54 ◽  
Author(s):  
E. Nabedryk ◽  
S. Andrianambinintsoa ◽  
G. Berger ◽  
M. Leonhard ◽  
W. Mäntele ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Ftir Spectroscopy ◽  
Reaction Center ◽  
Electron Acceptor

scholarly journals A Reaction Center-dependent Photoprotection Mechanism in a Highly Robust Photosystem II from an Extremophilic Red Alga,Cyanidioschyzon merolae

2013 ◽  
Vol 288 (32) ◽  
pp. 23529-23542 ◽  
Author(s):  
Tomasz Krupnik ◽  
Eva Kotabová ◽  
Laura S. van Bezouwen ◽  
Radosław Mazur ◽  
Maciej Garstka ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Red Alga ◽  
Cyanidioschyzon Merolae

Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10220-10226 ◽  
Author(s):  
Roberto Barbato ◽  
Giulia Friso ◽  
Maria Teresa Giardi ◽  
Fernanda Rigoni ◽  
Giorgio Mario Giacometti
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Degradation Products ◽  
D1 Protein

On the Question of the Chlorophyll a Content of the Photosystem II Reaction Center

1994 ◽  
Vol 98 (31) ◽  
pp. 7725-7735 ◽  
Author(s):  
H.-C. Chang ◽  
R. Jankowiak ◽  
N. R. S. Reddy ◽  
C. F. Yocum ◽  
R. Picorel ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Reaction Center ◽  
Chlorophyll A Content
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