Advanced

Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex

Hederstedt, Lars LU (1986) In Methods in Enzymology 126. p.399-414
Abstract
This chapter discusses the molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. The citric acid cycle enzyme succinate dehydrogenase (SDH) is a membrane-bound iron-sulfur flavoprotein. Mitochondrial and bacterial SDH and membrane-bound fumarate reductase in anaerobic and facultative bacteria are similar in composition. SDH and also fumarate reductase can be extracted with detergent from the membrane in a complex with one or two (depending on the organism) small hydrophobic polypeptides. These small associated polypeptides are integral membrane proteins that anchor each enzyme to the membrane and are, at least in mitochondria, required for electron transfer from enzyme to quinone. The... (More)
This chapter discusses the molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. The citric acid cycle enzyme succinate dehydrogenase (SDH) is a membrane-bound iron-sulfur flavoprotein. Mitochondrial and bacterial SDH and membrane-bound fumarate reductase in anaerobic and facultative bacteria are similar in composition. SDH and also fumarate reductase can be extracted with detergent from the membrane in a complex with one or two (depending on the organism) small hydrophobic polypeptides. These small associated polypeptides are integral membrane proteins that anchor each enzyme to the membrane and are, at least in mitochondria, required for electron transfer from enzyme to quinone. The chapter discusses about the (1) growth of B. subtilis and isolation of membranes, (2) immunoprecipitation and composition of B. subtilis SDH Complex, (3) genetics of B. subtilis SDH-protoplast fusion, and (4) biosynthesis of SDH Complex. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
in
Methods in Enzymology
volume
126
pages
399 - 414
publisher
Academic Press
external identifiers
  • scopus:0022822105
ISSN
0076-6879
DOI
10.1016/S0076-6879(86)26040-1
language
English
LU publication?
no
id
cf46fba3-5796-4634-acdf-dfa4d578d20e
date added to LUP
2017-07-18 11:05:27
date last changed
2017-10-15 04:53:07
@article{cf46fba3-5796-4634-acdf-dfa4d578d20e,
  abstract     = {This chapter discusses the molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex. The citric acid cycle enzyme succinate dehydrogenase (SDH) is a membrane-bound iron-sulfur flavoprotein. Mitochondrial and bacterial SDH and membrane-bound fumarate reductase in anaerobic and facultative bacteria are similar in composition. SDH and also fumarate reductase can be extracted with detergent from the membrane in a complex with one or two (depending on the organism) small hydrophobic polypeptides. These small associated polypeptides are integral membrane proteins that anchor each enzyme to the membrane and are, at least in mitochondria, required for electron transfer from enzyme to quinone. The chapter discusses about the (1) growth of B. subtilis and isolation of membranes, (2) immunoprecipitation and composition of B. subtilis SDH Complex, (3) genetics of B. subtilis SDH-protoplast fusion, and (4) biosynthesis of SDH Complex.},
  author       = {Hederstedt, Lars},
  issn         = {0076-6879},
  language     = {eng},
  pages        = {399--414},
  publisher    = {Academic Press},
  series       = {Methods in Enzymology},
  title        = {Molecular properties, genetics, and biosynthesis of <em>Bacillus subtilis</em> succinate dehydrogenase complex},
  url          = {http://dx.doi.org/10.1016/S0076-6879(86)26040-1},
  volume       = {126},
  year         = {1986},
}