Environment and Function of the Redox Active Tyrosines of Photosystem II

1995 ◽  
pp. 1207-1212 ◽  
Author(s):  
Bruce A. Diner ◽  
Xiao-Song Tang ◽  
Ming Zheng ◽  
G. Charles Dismukes ◽  
Dee Ann Force ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Redox Active ◽  
And Function

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.

Light stress provokes plastic and elastic modifications in structure and function of photosystem II in camellia leaves

1997 ◽  
Vol 101 (2) ◽  
pp. 265-277 ◽  
Author(s):  
Gert H. J. Kruger ◽  
Merope Tsimilli-Michael ◽  
Reto J. Strasser
Keyword(s):  
Photosystem Ii ◽  
Light Stress ◽  
Structure And Function ◽  
And Function

Steric and Electronic Effects of Ligand Substitution on Redox-Active Fe4S4-Based Coordination Polymers

2021 ◽  
Author(s):  
Omar Salinas ◽  
Jiaze Xie ◽  
Robert Papoular ◽  
Noah Horwitz ◽  
Erik Elkaim ◽  
...  
Keyword(s):  
Coordination Polymers ◽  
Ligand Substitution ◽  
Molecular Materials ◽  
Electronic Effects ◽  
Redox Active ◽  
And Function ◽  
Structure Properties

One of the notable advantages of molecular materials is the ability to precisely tune structure, properties, and function via molecular substitutions. While many studies have demonstrated this principle with classic...

scholarly journals The encapsulin from Thermatoga maritima is a flavoprotein with a symmetry matched ferritin-like cargo protein

2021 ◽  
Author(s):  
Benjamin J LaFrance ◽  
Caleb Cassidy-Amstutz ◽  
Robert J Nichols ◽  
Luke M Oltrogge ◽  
Eva Nogales ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Biochemical Analysis ◽  
Active Role ◽  
Structure And Function ◽  
Redox Active ◽  
Cargo Protein ◽  
Cargo Proteins ◽  
And Function ◽  
Flavin Binding ◽  
Unique Chemical

Bacterial nanocompartments, also known as encapsulins, are an emerging class of protein-based "organelles" found in bacteria and archaea. Encapsulins are virus-like icosahedral particles comprising a ~25-50 nm shell surrounding a specific cargo enzyme. Compartmentalization is thought to create a unique chemical environment to facilitate catalysis and isolate toxic intermediates. Many questions regarding nanocompartment structure-function remain unanswered, including how shell symmetry dictates cargo loading and to what extent the shell facilitates enzymatic activity. Here, we explore these questions using the model T. maritima nanocompartment known to encapsulate a redox-active ferritin-like protein. Biochemical analysis revealed the encapsulin shell to possess a flavin binding site located at the interface between capsomere subunits, suggesting the shell may play a direct and active role in the function of the encapsulated cargo. Furthermore, we used cryoEM to show that cargo proteins use a form of symmetry-matching to facilitate encapsulation and define stoichiometry. In the case of the T. maritima encapsulin, the decameric cargo protein with 5-fold symmetry preferentially binds to the pentameric-axis of the icosahedral shell. Taken together, these observations suggest the shell is not simply a passive barrier-it also plays a significant role in the structure and function of the cargo enzyme.

scholarly journals Carotenoids Assist in Cyanobacterial Photosystem II Assembly and Function

2016 ◽  
Vol 7 ◽  
Author(s):  
Tomas Zakar ◽  
Hajnalka Laczko-Dobos ◽  
Tunde N. Toth ◽  
Zoltan Gombos
Keyword(s):  
Photosystem Ii ◽  
And Function

Polypeptides of Photosystem II: Structure and function

1999 ◽  
pp. 264-291 ◽  
Author(s):  
Demetrios F. Ghanotakis ◽  
Georgios Tsiotis ◽  
Terry M. Bricker
Keyword(s):  
Photosystem Ii ◽  
Structure And Function ◽  
And Function

Thoughts Concerning a New Paradigm of the Photosystem II Region of the Thylakoid Membrane Based on Lipid Structure and Function

1995 ◽  
pp. 170-172 ◽  
Author(s):  
Paul-André Siegenthaler ◽  
Yinong Xu ◽  
Jana Smutny ◽  
Marlyse Meylan Bettex ◽  
Jarmila Vallino ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
Structure And Function ◽  
New Paradigm ◽  
Lipid Structure ◽  
And Function

On the Binding and Function of Chloride in Photosystem II

1995 ◽  
pp. 1379-1382
Author(s):  
K. Lindberg ◽  
L.-E. Andréasson
Keyword(s):  
Photosystem Ii ◽  
And Function
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