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Biochemical and biophysical studies of the E. coli respiratory chain

Technical Report ·
OSTI ID:5464494
E. coli contains two distinct ubiquinol oxidases but contains no cytochrome c-dependent branch of its aerobic respiratory chain. The cytochrome d complex has a very high affinity for molecular oxygen and is the predominant oxidase when the cells are grown with limited oxygen. The cytochrome o complex is the predominant oxidase present when E. coli is grown at high aeration. This grant is directed towards characterizing the cytochrome o complex. Substantial progress has been made during the past five years. The single most important results of our work is the demonstration that the E. coli cytochrome o complex is closely related structurally to the family of mitochondrial and bacterial aa{sub 3}-type cytochrome c oxidases. This has revealed the existence of a superfamily of proton-pumping respiratory oxidases that share common structural and mechanistic features, but vary with respect to substrate (cytochrome c vs quinol) and/or heme components (a-type vs protoheme). 55 refs., 8 figs.
Research Organization:
Illinois Univ., Urbana, IL (United States). Dept. of Chemistry
Sponsoring Organization:
DOE; USDOE, Washington, DC (United States)
DOE Contract Number:
FG02-87ER13716
OSTI ID:
5464494
Report Number(s):
DOE/ER/13716-2; ON: DE91016966
Country of Publication:
United States
Language:
English

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