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

Lars Hederstedt

Journal: Biochimica et biophysica acta 2002;1553(1-2):74-83

PMID: 11803018

Free Full Text on Elsevier Science View on PubMed

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.

Address: Department of Microbiology, Lund University, Sölvegatan 12, SE-223 62, Lund, Sweden. [email protected]

DOI: 10.1016/s0005-2728(01)00231-6

Link outs

Free resources

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0005...

Molecular Biology Databases:

https://biocyc.org/gene?orgid=BSUB&id=BSU28430

MeSH Terms: Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Carboxin, Drug Resistance, Microbial, Electron Transport Complex II, Enzyme Inhibitors, Hydroxyquinolines, Intracellular Membranes, Membrane Potentials, Membrane Proteins, Molecular Sequence Data, Multienzyme Complexes, Oxidoreductases, Paracoccus denitrificans, Quinone Reductases, Sequence Alignment, Succinate Dehydrogenase