scholarly journals Proton-Coupled Electron Transfer and Redox-Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II

2012 ◽  
Vol 3 (4) ◽  
pp. 543-554 ◽  
Author(s):  
Bridgette A. Barry ◽  
Jun Chen ◽  
James Keough ◽  
David Jenson ◽  
Adam Offenbacher ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Ribonucleotide Reductase ◽  
Structure And Function ◽  
Proton Coupled Electron Transfer ◽  
Redox Active ◽  
Tyrosyl Radicals ◽  
And Function

Proton-Coupled Electron-Transfer Processes in Photosystem II Probed by Highly Resolvedg-Anisotropy of Redox-Active Tyrosine YZ

2011 ◽  
Vol 133 (12) ◽  
pp. 4655-4660 ◽  
Author(s):  
Hideto Matsuoka ◽  
Jian-Ren Shen ◽  
Asako Kawamori ◽  
Kei Nishiyama ◽  
Yasunori Ohba ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Transfer Processes ◽  
Proton Coupled Electron Transfer ◽  
Redox Active ◽  
Electron Transfer Processes

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

Proton-Coupled Electron Transfer and Tyrosine D of Photosystem II

2007 ◽  
Vol 111 (43) ◽  
pp. 12599-12604 ◽  
Author(s):  
David L. Jenson ◽  
Amaris Evans ◽  
Bridgette A. Barry
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Proton Coupled Electron Transfer ◽  
Tyrosine D

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.

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