Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation

  title={Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation},
  author={Victoria Yankovskaya and Rob Horsefield and Susanna T{\"o}rnroth and Cesar Luna-Chavez and Hideto Miyoshi and Christophe L{\'e}ger and Bernadette Byrne and Gary Cecchini and So Iwata},
  pages={700 - 704}
The structure of Escherichia colisuccinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during… 
Escherichia coli succinate dehydrogenase variant lacking the heme b
It is indicated that redox cycling of the heme in complex II is not essential for the enzyme's ubiquinol reductase activity and the mutants lacking heme are highly sensitive to the presence of detergent.
Succinate dehydrogenase: the complex roles of a simple enzyme.
Analysis of Mammalian Succinate Dehydrogenase Kinetics and Reactive Oxygen Species Production
A computational model is developed to analyze free radical production data from complex II and identify the mechanism of superoxide and hydrogen peroxide production and highlights the importance of evaluating enzyme kinetics and associated side-reactions in a consistent, quantitative and biophysical detailed manner.
Complex II Is Complex Too
The crystal structure of bacterial SQR (equivalent to mitochondrial complex II) reveals how the arrangement of redox centers in this enzyme enables electrons to be transferred to ubiquinone while minimizing production of reactive oxygen species that could damage tissues.
Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction
It is found that numerous anticancer drugs and cytokines such as Fas ligand and tumour necrosis factor α provoke intracellular acidification and cause the formation of mitochondrial ROS and the succinate:ubiquinone oxidoreductase (SQR) activity of the mitochondrial respiratory complex II is specifically impaired.
The Superfamily of Succinate:Quinone Oxidoreductases and its Implications for the Cyanobacterial Enzymes
QFR and SQR complexes, collectively referred to as succinate:quinone oxidoreductases (EC, have very similar compositions and are predicted to share similar structures.


Structure of the Escherichia coli fumarate reductase respiratory complex.
The crystal structure of intact fumarate reductase has been solved at 3.3 angstrom resolution and demonstrates that the cofactors are arranged in a nearly linear manner from the membrane-bound quinone to the active site flavin.
Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
The crystal structure of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes is described and a pathway of electron transfer from the dihaem cytochrome b to the site offumarate reduction and a mechanism of fUMarate reduction is proposed.
Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N
The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined and provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.
Expression and functional properties of fumarate reductase.
INTRODUCTION Fumarate reductase (FRD) catalyses the reduction of fumarate to succinate and is a key enzyme for the anaerobic functioning of many organisms respiring with fumarate as terminal electron
Interactions of oxaloacetate with Escherichia coli fumarate reductase.
Mechanism of Superoxide and Hydrogen Peroxide Formation by Fumarate Reductase, Succinate Dehydrogenase, and Aspartate Oxidase*
Characteristics of Frd suggest that all detectable autoxidation occurs from its FAD site, rather than from iron-sulfur clusters or bound quinones, and this model is supported by the behavior of “ aspartate oxidase” (aspartate:fumarate oxidoreductase), an Frd homologue that lacks Fe-S clusters.
Respiration Without O2
The crystal structure of fumarate reductase, reported in this issue by Iverson, is the first structure of the important respiration chain enzymes that catalyze succinate-fumarate interconversion
A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes
The results indicate that mev-1 governs the rate of ageing by modulating the cellular response to oxidative stress, which may cause an indirect increase in superoxide levels, which in turn leads to oxygen hypersensitivity and premature ageing.
Inhibitor Probes of the Quinone Binding Sites of Mammalian Complex II and Escherichia coli Fumarate Reductase*
2-alkyl-4,6-dinitrophenols turned out to be even more potent inhibitors of E. coli fumarate reductase, particularly when acting in the direction of quinol oxidation, again, the physiological event.