Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli

This publication has 27 references indexed in Scilit:

• 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
• Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1987
• 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
• Assignment of ESR signals of Escherichia coli terminal oxidase complexes
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1985
• Effects of pH and detergent on the kinetic and electrochemical properties of the purified cytochrome d terminal oxidase complex of Escherichia coli
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
• Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli.
  Biochemistry, 1984
• Resonance Raman spectroscopy of an oxygenated intermediate species of cytochrome oxidasedfromEscherichia coli
  FEBS Letters, 1982
• Trapping of an intermediate in the oxidation‐reduction cycle of cytochrome d in Escherichia coli
  FEBS Letters, 1976