Respiration and Energy Transduction in Escherichia coli

Hendler, Richard W.

doi:10.1007/978-1-4684-2658-8_4

Cited by 2 publications

(3 citation statements)

References 120 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This cytochrome is thought to be reduced by succinate via succinate dehydrogenase. An association between cytochrome b and succinate dehydrogenase has been suggested for several bacterial species (9,12). In analogy with complex II (succinate-ubiquinone reductase) from beef heart mitochondria (11), the B. subtilis SDH complex contains 1 mol of cytochrome per mol of flavin.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100

Hederstedt¹,

Holmgren²,

Rutberg³

1979

J Bacteriol

View full text Add to dashboard Cite

A succinic dehydrogenase (SDH) complex has been purified from Triton X-100-solubilized membranes from Bacillus subtilis by precipitation with specific antibody. Radioactively labeled precipitated complex was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by autoradiography of the gels. The complex contained equimolar amounts of three polypeptides with approximate molecular weights of 65,000, 28,000, and 19,000. Five succinic dehydrogenase-negative mutants, belonging to the citF group, contained the 65,000dalton polypeptide in a soluble form in the cytoplasm. Each 65,000-dalton polypeptide had about one molecule of flavin bound. Another citF mutant, citFIl, which lacks the 65,000-dalton polypeptide, contained a membrane-bound 28,000dalton polypeptide. The wild-type succinic dehydrogenase complex contained cytochrome, probably a cytochrome b. The 19,000-dalton polypeptide is suggested to represent the apoprotein of this cytochrome. The 65,000-dalton and the 28,000dalton polypeptides are thought to constitute succinic dehydrogenase and to correspond to the flavoprotein and the ironprotein, respectively, as described for succinic dehydrogenase isolated from beef heart mitochondria or Rhodospirillum rubrum chromatophores. The results presented suggest that in B. subtilis succinic dehydrogenase is attached to a cytochrome b in the membrane via the 28,000dalton (ironprotein) polypeptide. Succinic dehydrogenase (SDH) [EC 1.3.99.1, succinate:(acceptor) oxidoreductase] is a firmly membrane-bound enzyme in Bacillus subtilis and other aerobic bacteria. It can be solubilized with nonionic detergents in an active form (18). We have recently solubilized an SDH complex from B. subtilis membranes and characterized the solubilized proteins in crossed immunoelectrophoresis (CIE). Among a number of precipitates obtained with an antiserum prepared against whole membranes, one was identified as containing SDH. No precipitate staining for SDH was found in CIE of membranes from nine SDH mutants (18). The respective mutations of these mutants all map in a region called citF (17). An SDH-specific antiserum was obtained by immunizing rabbits with the SDH precipitate from CIE. This antiserum was used to identify a soluble SDH antigen in five of the nine citF mutants. Wild-type bacteria contain little soluble SDH antigen.In the present experiments, we have used the SDH-specific antiserum to isolate and characterize the solubilized SDH complex in B. subtilis. The experiments give information about the possible subunit structure of the enzyme and about binding of the enzyme to the cytoplasmic membrane. The experiments also indicate that SDH, in the membrane, is closely associated with cytochrome. In an accompanying paper we will show that there is a close correlation between membrane binding of SDH and synthesis of heme in B. subtilis (13).MATERIALS AND METHODS Bacteria. B. subtilis BrlO2 (hisB trpC2) was used as the wild type; it was originally obtained from J. Spizizen. The SDH mutants (citF mutants) have been...

show abstract

Section: Discussionmentioning

confidence: 99%

Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100

Hederstedt¹,

Holmgren²,

Rutberg³

1979

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…If these same conditions did not result in an elevated level of cAMP, then it would be possible to conclude that an energy demand, and not high cAMP levels, was responsible for the induction of threonine dehydratase. Cyanide is a potent inhibitor of respiratory processes by virtue of its interaction with a terminal oxidase (14) and thus forces a halt to ATP synthesis from oxidative phosphorylation. When a culture of E. coli growing on GF medium plus threonine under vigorous aerobic conditions was exposed to 2.5 mM potassium cyanide, growth was quickly arrested but resumed slowly after 30 min (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The pyruvate formate-lyase of E. coli is known to be active only under anaerobic conditions although it is produced in an inactive form during aerobic growth (15). This sequence of reactions could be used for temporary ATP production before the full development of ATP synthesis from anaerobic electron transport-mediated processes linked to the ultimate reduction of fumarate, nitrate, or protons via anaerobic cytochrome systems (13,14).…”

mentioning

confidence: 99%

Control of biodegradative threonine dehydratase inducibility by cyclic AMP in energy-restricted Escherichia coli

Phillips¹,

Egan²,

Lewis³

1978

J Bacteriol

View full text Add to dashboard Cite

To explain the requirement for anaerobic conditions in the induction of biodegradative L-threonine dehydratase in Escherichia coli, Crookes strain, measurements of cyclic AMP (cAMP) were made during aerobic and anaerobic growth and upon an aerobic-to-anaerobic transition. Internal cAMP levels were similar (5 to 10 pM) throughout exponential growth, whether aerobic or anaerobic, but only during anaerobiosis was threonine dehydratase synthesized. When an exponentially growing aerobic culture was made anaerobic, a sharp increase in internal cAMP was noted, reaching 300 FM within 10 min and declining thereafter to normal anaerobic levels. Threonine dehydratase synthesis was detected immediately after the attainment of peak cAMP levels and continued for several generations A similar pattern but with less accumulation of cAMP and less threonine dehydratase production was also noted upon treatment ofan aerobicaUy growing culture with KCN. Pyruvate addition at the time of anaerobic shock severely affected both cAMP accumulation and threonine dehydratase synthesis; *however, externally added cAMP could parially counter the pyruvate effect on enzyme synthesis. The conclusion was reached that conditions which resulted in a temporary energy deficit brought about the major accumulation of cAMP, and this elevated level served as a signal for initiation of teonine dehydratase synthesis to supply energy by the nonoxidative degradation of threonine.

show abstract

Respiration and Energy Transduction in Escherichia coli

Cited by 2 publications

References 120 publications

Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100

Characterization of a succinate dehydrogenase complex solubilized from the cytoplasmic membrane of Bacillus subtilis with the nonionic detergent Triton X-100

Control of biodegradative threonine dehydratase inducibility by cyclic AMP in energy-restricted Escherichia coli

Contact Info

Product

Resources

About