Molecular properties, genetics, and biosynthesis of Bacillus subtilis succinate dehydrogenase complex
(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)
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- author
- Hederstedt, Lars LU
- publishing date
- 1986
- 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
- 2024-01-14 00:58:28
@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}}, doi = {{10.1016/S0076-6879(86)26040-1}}, volume = {{126}}, year = {{1986}}, }