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Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis.

Hederstedt, Lars LU (2002) In Biochimica et Biophysica Acta (BBA) - Bioenergetics 1553(1-2). p.74-83
Abstract
An overview of the present knowledge about succinate:quinone oxidoreductase in Paracoccus denitrificans and Bacillus subtilis is presented. P. denitrificans contains a monoheme succinate:ubiquinone oxidoreductase that is similar to that of mammalian mitochondria with respect to composition and sensitivity to carboxin. Results obtained with carboxin-resistant P. denitrificans mutants provide information about quinone-binding sites on the enzyme and the molecular basis for the resistance. B. subtilis contains a diheme succinate:menaquinone oxidoreductase whose activity is dependent on the electrochemical gradient across the cytoplasmic membrane. Data from studies of mutant variants of the B. subtilis enzyme combined with available crystal... (More)
An overview of the present knowledge about succinate:quinone oxidoreductase in Paracoccus denitrificans and Bacillus subtilis is presented. P. denitrificans contains a monoheme succinate:ubiquinone oxidoreductase that is similar to that of mammalian mitochondria with respect to composition and sensitivity to carboxin. Results obtained with carboxin-resistant P. denitrificans mutants provide information about quinone-binding sites on the enzyme and the molecular basis for the resistance. B. subtilis contains a diheme succinate:menaquinone oxidoreductase whose activity is dependent on the electrochemical gradient across the cytoplasmic membrane. Data from studies of mutant variants of the B. subtilis enzyme combined with available crystal structures of a similar enzyme, Wolinella succinogenes fumarate reductase, substantiate a proposed explanation for the mechanism of coupling between quinone reductase activity and transmembrane potential. (Less)
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@misc{31160cd5-7fcf-4528-ad96-4f6f73bf529f,
  abstract     = {An overview of the present knowledge about succinate:quinone oxidoreductase in Paracoccus denitrificans and Bacillus subtilis is presented. P. denitrificans contains a monoheme succinate:ubiquinone oxidoreductase that is similar to that of mammalian mitochondria with respect to composition and sensitivity to carboxin. Results obtained with carboxin-resistant P. denitrificans mutants provide information about quinone-binding sites on the enzyme and the molecular basis for the resistance. B. subtilis contains a diheme succinate:menaquinone oxidoreductase whose activity is dependent on the electrochemical gradient across the cytoplasmic membrane. Data from studies of mutant variants of the B. subtilis enzyme combined with available crystal structures of a similar enzyme, Wolinella succinogenes fumarate reductase, substantiate a proposed explanation for the mechanism of coupling between quinone reductase activity and transmembrane potential.},
  author       = {Hederstedt, Lars},
  keyword      = {Succinate Dehydrogenase/antagonists & inhibitors/chemistry/*metabolism,Molecular Sequence Data,Support,Non-U.S. Gov't,Membrane Proteins/chemistry/metabolism,Membrane Potentials,Hydroxyquinolines/pharmacology,Enzyme Inhibitors/pharmacology,Intracellular Membranes/chemistry/enzymology,Microbial,Amino Acid Sequence,Drug Resistance,Bacillus subtilis/drug effects/*enzymology/genetics,Carboxin/pharmacology,Sequence Alignment,Quinone Reductases/chemistry/metabolism,Paracoccus denitrificans/drug effects/*enzymology/genetics,Oxidoreductases/antagonists & inhibitors/chemistry/*metabolism,Multienzyme Complexes/antagonists & inhibitors/chemistry/*metabolism,Comparative Study},
  language     = {eng},
  number       = {1-2},
  pages        = {74--83},
  publisher    = {ARRAY(0xc4b3468)},
  series       = {Biochimica et Biophysica Acta (BBA) - Bioenergetics},
  title        = {Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis.},
  url          = {http://dx.doi.org/10.1016/S0005-2728(01)00231-6},
  volume       = {1553},
  year         = {2002},
}