Interaction of Cytochrome bd with Carbon Monoxide at Low and Room Temperatures

This publication has 42 references indexed in Scilit:

• Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli
  Biochemistry, 1995
• Cyanide‐reactive sites in cytochrome bd complex from E. coli
  FEBS Letters, 1993
• Properties of the two terminal oxidases of Escherichia coli
  Biochemistry, 1991
• 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
• Bacterial proteins with co-binding b- or c-type haem fucntions and absorption spectroscopy
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
• Photolysis at very low temperatures of co‐liganded cytochrome oxidase (cytochrome d) in oxygen‐limited Escherichia coli
  FEBS Letters, 1982
• The Light-reversible Binding of Carbon Monoxide to Cytochrome a1 in Escherichia coli K12
  Microbiology, 1981