Properties of the two terminal oxidases of Escherichia coli

• Published in: Biochemistry (Easton) Vol. 30; no. 16; pp. 3936 - 3942
• Main Authors: Puustinen, Anne, Finel, Moshe, Haltia, Tuomas, Gennis, Robert B, Wikstrom, Marten
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 23.04.1991
• Subjects: 550200 - Biochemistry; ABSORPTION SPECTRA; BACTERIA; BASIC BIOLOGICAL SCIENCES; BIOCHEMISTRY; Biological and medical sciences; Cardiolipins; CELL CONSTITUENTS; CELL MEMBRANES; Cell structures and functions; CHEMISTRY; CYTOCHROME OXIDASE; CYTOCHROMES; ELECTRON SPECTRA; Electron Spin Resonance Spectroscopy; Electron Transport Complex IV - isolation & purification; Electron Transport Complex IV - metabolism; ENZYMES; ESCHERICHIA COLI; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; HAEM DEHYDROGENASES; Hydrogen-Ion Concentration; Kinetics; LIPOSOMES; MEMBRANES; MICROORGANISMS; Mitochondria and cell respiration; Molecular and cellular biology; ORGANIC COMPOUNDS; OXIDOREDUCTASES; Oxygen Consumption; PIGMENTS; PROTEINS; Proteolipids - metabolism; REDOX POTENTIAL; SPECTRA; Spectrophotometry; Spheroplasts - enzymology; Cytochrome; Purification; Escherichia coli; EPR spectrometry; Proton transfer; Liposome; Enzymatic activity; Polarography; Reconstituted system; Reaction mechanism; Bacteria; Chemical composition; Mutation; Enterobacteriaceae

Proton translocation coupled to oxidation of ubiquinol by O2 was studied in spheroplasts of two mutant strains of Escherichia coli, one of which expresses cytochrome d, but not cytochrome bo, and the other expressing only the latter. O2 pulse experiments revealed that cytochrome d catalyzes separati...