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Succinate dehydrogenase and fumarate reductase from Escherichia coli.
TLDR
The structure and function of SQR and QFR are briefly summarized in this communication and the similarities and differences in the membrane domain of the two enzymes are discussed.
Structure of Escherichia coli Succinate:Quinone Oxidoreductase with an Occupied and Empty Quinone-binding Site*
TLDR
The dicarboxylate-binding site in the soluble domain of SQR is highly similar to that seen in high resolution structures of avian SQR and soluble flavocytochrome c (PDB 1QJD) showing mechanistically significant structural features conserved across prokaryotic and eukaryotic SQRs.
Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from
TLDR
The kinetic properties of SQR and QFR suggest that either ubiquinone or menaquinone operates at a single exchangeable site working in forward or reverse reactions, suggesting the importance of similar catalytic groups in quinol deprotonation and oxidation.
Effect of oxygen on activation state of complex I and lack of oxaloacetate inhibition of complex II in Langendorff perfused rat heart
TLDR
The findings indicate that the state of activation of complex I is controlled by the oxygen saturation in the perfusate, and show that complex II is fully active in the mitochondrion and not inhibited by OAA regardless of the oxygen concentration.
Anaerobic Expression of Escherichia coli Succinate Dehydrogenase: Functional Replacement of Fumarate Reductase in the Respiratory Chain during Anaerobic Growth
TLDR
It was found that, under anaerobic growth conditions where fumarate is utilized as the terminal electron acceptor, SQR would function to support anaerilic growth of E. coli.
The Quinone Binding Site in Escherichia coli Succinate Dehydrogenase Is Required for Electron Transfer to the Heme b*
TLDR
The results demonstrate the importance of a functional, semiquinone-stabilizing QP site for the observation of rapid succinate-dependent heme reduction and the mutations result in the elimination of EPR-visible ubisemiquin one during potentiometric titrations.
A Novel Intracellular Isoform of Matrix Metalloproteinase-2 Induced by Oxidative Stress Activates Innate Immunity
TLDR
A novel N-terminal truncated intracellular isoform of MMP-2 is induced by oxidative stress and initiates a primary innate immune response that may contribute to progressive cardiac dysfunction in the setting of ischemia and systolic failure.
The quinone-binding and catalytic site of complex II.
TLDR
Comparisons of the structures of the quinone binding sites in SQR and QFR reveal how the enzymes have adapted in order to accommodate both benzo- and napthoquinones, and suggest that movement of theQuinone within the Quinone-binding pocket is essential for catalysis.
Effect of anoxia/reperfusion on the reversible active/de-active transition of NADH-ubiquinone oxidoreductase (complex I) in rat heart.
TLDR
Studying the effect of anoxia and reperfusion on the A/D-equilibrium of complex I in rat hearts ex vivo finds abrupt alternation of anoxic and normoxic perfusion allows cycling between the two states of the enzyme.
Active/de-active transition of respiratory complex I in bacteria, fungi, and animals.
TLDR
It was found that complex I from the bacterium Escherichia coli and from non-vertebrate organisms did not show the A/D transitions, and it was shown that the lower eukaryotes, Neurospora crassa and Yarrowia lipolytica, exhibited very distinct A-D transitions with much lower activation barriers compared to the bovine enzyme.
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