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The Journal of Cell Biology, Vol 55, 266-281, Copyright © 1972 by Rockefeller University Press

ARTICLE

RESPIRATION AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI MEMBRANE-ENVELOPE FRAGMENTS : VI. Solubilization and Characterization of the Electron Transport Chain



Richard W. Hendler 1 and Amelia H. Burgess 1

1 From the Laboratory of Biochemistry, Section on Cellular Physiology, National Heart and Lung Institute, Bethesda, Maryland 20014

Membranes obtained from Escherichia coli have been solubilized with deoxycholate. The solubilized dehydrogenases and cytochromes are not sedimented at 105,000 g. These components readily penetrate the "included space" of Sepharose 4B (Pharmacia Fine Chemicals Inc., Uppsala, Sweden) and polyacrylamide gels and have been fractionated on the basis of molecular size. Solubilization destroys nicotinamide adenine dinucleotide, reduced form (NADH) oxidase and D-lactate oxidase activities, but leaves an appreciable part of the original succinoxidase activity intact. Evidence for a succinate dehydrogenase-cytochrome b1 complex is given. Menadione added to the solubilized preparation does not elicit NADH oxidase activity nor stimulate the existing succinoxidase activity, but does provoke an active D-lactate oxidase activity. This D-lactate oxidase activity, however, does not use cytochromes and is not sensitive to cyanide.

Submitted on February 29, 1972
Revised on June 15, 1972


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