Succinate dehydrogenase in Rhodopseudomonas sphaeroides: subunit composition and immunocross-reactivity with other related bacteria

J Bacteriol. 1985 Aug;163(2):778-82. doi: 10.1128/jb.163.2.778-782.1985.

Abstract

Antibodies were raised against the succinate dehydrogenase (SDH) present in the chromatophores of phototrophically grown Rhodopseudomonas sphaeroides. Crossed immunoelectrophoresis experiments indicated that the SDH present in the cytoplasmic membranes of heterotrophically grown R. sphaeroides is probably the same enzyme observed in the chromatophores. The enzyme was extracted by Triton X-100 in a form which consisted of only two subunits (molecular weight, 68,000 and 30,000) and was not associated with a cytochrome b. The antibodies directed against SDH from R. sphaeroides showed no immunocross-reactivity with SDH from phylogenetically related bacterial species, including Rhodopseudomonas capsulata, Paracoccus denitrificans, Rhodopseudomonas palustris, Rhodospirillum rubrum, and Rhodospirillum fulvum.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Chromatophores / enzymology
  • Cell Membrane / enzymology
  • Cross Reactions
  • Immune Sera
  • Immunoelectrophoresis
  • Macromolecular Substances
  • Molecular Weight
  • Paracoccus denitrificans / enzymology
  • Rhodobacter sphaeroides / enzymology*
  • Rhodopseudomonas / enzymology
  • Rhodospirillum / enzymology
  • Species Specificity
  • Succinate Dehydrogenase / isolation & purification*

Substances

  • Immune Sera
  • Macromolecular Substances
  • Succinate Dehydrogenase