Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize functional domain.

This publication has 27 references indexed in Scilit:

• The two terminal oxidases of the aerobic respiratory chain of Escherichiacoli each yield water and not peroxide as a final product
  Biochemical and Biophysical Research Communications, 1988
• Formation of the 680 nm‐absorbing form of the cytochrome bd oxidase complex of Escherichia coli by reaction of hydrogen peroxide with the ferric form
  FEBS Letters, 1988
• Proposal that the function of the membrane‐bound cytochrome a₁‐like haemoprotein (cytochrome b‐595) in Escherichia coli is a direct electron donation to cytochrome d
  FEBS Letters, 1987
• Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595
  Biochemistry, 1986
• Specific overproduction and purification of the cytochrome b558 component of the cytochrome d complex from Escherichia coli
  Biochemistry, 1986
• The oxygen reaction of the cytochrome d‐terminated respiratory chain of Escherichia coli at sub‐zero temperatures
  FEBS Letters, 1985
• Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli.
  Biochemistry, 1984
• Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase
  Biochemistry, 1984
• Resonance Raman spectroscopy of an oxygenated intermediate species of cytochrome oxidasedfromEscherichia coli
  FEBS Letters, 1982
• Electrochemical proton gradient in inverted membrane vesicles from Escherichia coli
  Biochemistry, 1980