scholarly journals Symmetry-related mutants in the quinone binding sites of the reaction center -- The effects of changes in charge distribution

1997 ◽  
Author(s):  
D.K. Hanson ◽  
M. Schiffer
Keyword(s):  
Charge Distribution ◽  
Reaction Center ◽  
Binding Sites ◽  
Quinone Binding

A Contact Site between the Two Reaction Center Polypeptides of Photosystem II Is Involved in Photoinhibition

1991 ◽  
Vol 46 (7-8) ◽  
pp. 557-562 ◽  
Author(s):  
A. Trebst
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Binding Sites ◽  
Cleavage Site ◽  
Amino Acid Sequences ◽  
Contact Site ◽  
Quinone Binding ◽  
Herbicide Binding ◽  
Sensitive Site

Abstract A new contact site between the two reaction center polypeptides D 1 and D 2 of photosystem II close to arg 238 and arg 234 respectively is proposed. The amino acid sequences involved are between the 4 th transmembrane and a connecting parallel helix. The sequence includes a tryp­ sin sensitive site in both polypeptides, the likely cleavage site in the rapid turnover of the D 1 polypeptide and part of the herbicide binding site. The contact site is oriented towards both quinone binding sites Q A and Q B. A folding of the backbone of the amino acid sequences involved is proposed.

scholarly journals Identification of FTIR Bands Due to Internal Water Molecules around the Quinone Binding Sites in the Reaction Center fromRhodobacter sphaeroides†

Biochemistry ◽  
2009 ◽  
Vol 48 (6) ◽  
pp. 1220-1229 ◽  
Author(s):  
Tatsuya Iwata ◽  
Mark L. Paddock ◽  
Melvin Y. Okamura ◽  
Hideki Kandori
Keyword(s):  
Reaction Center ◽  
Binding Sites ◽  
Water Molecules ◽  
Quinone Binding ◽  
Internal Water

scholarly journals Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels

2021 ◽  
Vol 7 (3) ◽  
pp. eabe2631
Author(s):  
David J. K. Swainsbury ◽  
Pu Qian ◽  
Philip J. Jackson ◽  
Kaitlyn M. Faries ◽  
Dariusz M. Niedzwiedzki ◽  
...  
Keyword(s):  
Binding Sites ◽  
Rhodopseudomonas Palustris ◽  
Ring Closure ◽  
Light Harvesting Complex ◽  
The Core ◽  
Quinone Binding ◽  
Cryo Electron Microscopy ◽  
Unique Protein ◽  
Center Light ◽  
Resolution Structure

The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo–electron microscopy structures of RC-LH1 complexes from Rhodopseudomonas palustris. A 2.65-Å resolution structure of the RC-LH114-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC QB site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange.

scholarly journals Two distinct binding sites for high potential iron-sulfur protein and cytochrome c on the reaction center-bound cytochrome of Rubrivivax gelatinosus.

2004 ◽  
Vol 279 (44) ◽  
pp. 46350
Author(s):  
Jean Alric ◽  
Makoto Yoshida ◽  
Kenji V.P. Nagashima ◽  
Rainer Hienerwadel ◽  
Pierre Parot ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Reaction Center ◽  
Binding Sites ◽  
High Potential ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Rubrivivax Gelatinosus

scholarly journals The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli

2010 ◽  
Vol 1797 (12) ◽  
pp. 1924-1932 ◽  
Author(s):  
Lai Lai Yap ◽  
Myat T. Lin ◽  
Hanlin Ouyang ◽  
Rimma I. Samoilova ◽  
Sergei A. Dikanov ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Ubiquinol Oxidase ◽  
Quinone Binding ◽  
Cytochrome Bo3
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