Flavohemoglobin Hmp, but Not Its Individual Domains, Confers Protection from Respiratory Inhibition by Nitric Oxide in Escherichia coli

This publication has 39 references indexed in Scilit:

• The X-ray Structure of Ferric Escherichia coliFlavohemoglobin Reveals an Unexpected Geometry of the Distal Heme Pocket
  Journal of Biological Chemistry, 2002
• Bacterial flavohaemoglobins: a consensus sequence and identification of a discrete enterobacterial group and of further bacterial globins
  FEMS Microbiology Letters, 1997
• Function and Expression of Flavohemoglobin in Saccharomyces cerevisiae
  Journal of Biological Chemistry, 1996
• The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition
  Microbiology, 1996
• The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo
  FEBS Letters, 1996
• NO at work
  Cell, 1994
• The haemoglobin‐like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C‐terminal domain shares homology with ferredoxin NADP⁺ reductases
  FEBS Letters, 1992
• Modified bacteriophage lambda promoter vectors for overproduction of proteins in Escherichia coli
  Gene, 1990
• Bacterial proteins with co-binding b- or c-type haem fucntions and absorption spectroscopy
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
• Studies on Yeast Hemoglobin
  European Journal of Biochemistry, 1973