The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli.
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چکیده
منابع مشابه
The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain.
The aerobic respiratory chain of Escherichia coli is branched. In aerobically grown cells harvested in midexponential phase, a respiratory chain containing only b-type cytochromes is predominant. This chain contains a terminal oxidase which is a b-type cytochrome, referred to as cytochrome o. However, when the bacteria are grown under conditions of oxygen limitation, additional components of th...
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Cytochrome bSh8-d complex, a terminal oxidase in the respiratory chain of Escherichia coli K12 grown under the condition of limited oxygen, was purified to near homogeneity. The purified oxidase complex is composed of equimolar amounts of two polypeptides, with M, = 26,000 and 51,000, determined with gel eIectrophoresis in the presence of sodium dodecyl sulfate. It contains 12.3 nmol of protohe...
متن کاملSupramolecular organizations in the aerobic respiratory chain of Escherichia coli.
The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species. Here we describe, for the first time, the identification of supramolecular organi...
متن کاملTerminal Oxidases of Escherichia coli Aerobic Respiratory Chain 11 . PURIFICATION AND PROPERTIES OF CYTOCHROME
Cytochrome bSh8-d complex, a terminal oxidase in the respiratory chain of Escherichia coli K12 grown under the condition of limited oxygen, was purified to near homogeneity. The purified oxidase complex is composed of equimolar amounts of two polypeptides, with M, = 26,000 and 51,000, determined with gel eIectrophoresis in the presence of sodium dodecyl sulfate. It contains 12.3 nmol of protohe...
متن کاملAerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode.
Escherichia coli is known to couple aerobic respiratory catabolism to ATP synthesis by virtue of the primary generators of the proton motive force-NADH dehydrogenase I, cytochrome bo(3), and cytochrome bd-I. An E. coli mutant deficient in NADH dehydrogenase I, bo(3) and bd-I can, nevertheless, grow aerobically on nonfermentable substrates, although its sole terminal oxidase cytochrome bd-II has...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)38675-1