scholarly journals Electron transfer activity through the quinone-binding site of complex II (succinate: Quinone reductase)

2010 ◽  
Vol 1797 ◽  
pp. 111
Author(s):  
Gary Cecchini ◽  
Elena Maklashina ◽  
Sujata S. Shinde ◽  
Robert F. Anderson ◽  
Russ Hille
Keyword(s):  
Electron Transfer ◽  
Binding Site ◽  
Quinone Reductase ◽  
Complex Ii ◽  
Transfer Activity ◽  
Quinone Binding

Molecular Modelling of the Interaction of Cyanoacrylate Inhibitors with Photosystem II Part 2. The Effect of Stereochemistry of Inhibitor Binding

1993 ◽  
Vol 48 (9-10) ◽  
pp. 782-787 ◽  
Author(s):  
Simon P. Mackay ◽  
Patrick J. O’Malley
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Binding Site ◽  
Energy Minimization ◽  
Electrostatic Interactions ◽  
D1 Protein ◽  
Spatial Arrangement ◽  
Inhibitor Binding ◽  
Protein Residues ◽  
Quinone Binding

Abstract The 2-cyanoacrylate inhibitors are a potent class of herbicides which block electron transfer in photosystem II. The spatial arrangement of different functional groups are an important factor in determining activity and a number of derivatives have been used as stereospecific probes of the secondary quinone binding site. More than one region of stereoselectivity in the binding site has been identified which influences the interaction with specific groups of the inhibitor. We have studied the interaction of various stereoisomers of the cyanoacrylates with the binding site in the D1 protein (residues Leu 210 to Val 280) by determining the nonbonded intermolecular energies between the modelled structures calculated by van der Waals and electrostatic interactions after energy minimization of the combined structures to reduce inter and intramolecular strain and have found that the results reflect the experimentally determined data

scholarly journals Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster

2021 ◽  
Vol 118 (15) ◽  
pp. e2022308118
Author(s):  
Xiaoting Zhou ◽  
Yan Gao ◽  
Weiwei Wang ◽  
Xiaolin Yang ◽  
Xiuna Yang ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Succinate Dehydrogenase ◽  
Krebs Cycle ◽  
Water Soluble ◽  
Electron Transfer Mechanism ◽  
Complex Ii ◽  
Electron Transfer Pathway ◽  
Quinone Binding ◽  
Reduction Activity ◽  
Quinone Reduction

Complex II, also known as succinate dehydrogenase (SQR) or fumarate reductase (QFR), is an enzyme involved in both the Krebs cycle and oxidative phosphorylation. Mycobacterial Sdh1 has recently been identified as a new class of respiratory complex II (type F) but with an unknown electron transfer mechanism. Here, using cryoelectron microscopy, we have determined the structure of Mycobacterium smegmatis Sdh1 in the presence and absence of the substrate, ubiquinone-1, at 2.53-Å and 2.88-Å resolution, respectively. Sdh1 comprises three subunits, two that are water soluble, SdhA and SdhB, and one that is membrane spanning, SdhC. Within these subunits we identified a quinone-binding site and a rarely observed Rieske-type [2Fe-2S] cluster, the latter being embedded in the transmembrane region. A mutant, where two His ligands of the Rieske-type [2Fe-2S] were changed to alanine, abolished the quinone reduction activity of the Sdh1. Our structures allow the proposal of an electron transfer pathway that connects the substrate-binding and quinone-binding sites. Given the unique features of Sdh1 and its essential role in Mycobacteria, these structures will facilitate antituberculosis drug discovery efforts that specifically target this complex.

scholarly journals Electron-Transfer Pathways in the Heme and Quinone-Binding Domain of Complex II (Succinate Dehydrogenase)

Biochemistry ◽  
2014 ◽  
Vol 53 (10) ◽  
pp. 1637-1646 ◽  
Author(s):  
Robert F. Anderson ◽  
Sujata S. Shinde ◽  
Russ Hille ◽  
Richard A. Rothery ◽  
Joel H. Weiner ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Succinate Dehydrogenase ◽  
Binding Domain ◽  
Complex Ii ◽  
Quinone Binding ◽  
Electron Transfer Pathways

scholarly journals Plasticity of the Quinone-binding Site of the Complex II Homolog Quinol:Fumarate Reductase

2013 ◽  
Vol 288 (34) ◽  
pp. 24293-24301 ◽  
Author(s):  
Prashant K. Singh ◽  
Maruf Sarwar ◽  
Elena Maklashina ◽  
Violetta Kotlyar ◽  
Sany Rajagukguk ◽  
...  
Keyword(s):  
Binding Site ◽  
Complex Ii ◽  
Quinone Binding

scholarly journals Structural and Computational Analysis of the Quinone-binding Site of Complex II (Succinate-Ubiquinone Oxidoreductase)

2005 ◽  
Vol 281 (11) ◽  
pp. 7309-7316 ◽  
Author(s):  
Rob Horsefield ◽  
Victoria Yankovskaya ◽  
Graham Sexton ◽  
William Whittingham ◽  
Kazuro Shiomi ◽  
...  
Keyword(s):  
Binding Site ◽  
Computational Analysis ◽  
Complex Ii ◽  
Ubiquinone Oxidoreductase ◽  
Quinone Binding

scholarly journals Perturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur Cluster

2011 ◽  
Vol 286 (14) ◽  
pp. 12756-12765 ◽  
Author(s):  
Jonathan Ruprecht ◽  
So Iwata ◽  
Richard A. Rothery ◽  
Joel H. Weiner ◽  
Elena Maklashina ◽  
...  
Keyword(s):  
Binding Site ◽  
Electronic Properties ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Complex Ii ◽  
Quinone Binding ◽  
Iron Sulfur
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