Electron paramagnetic resonance studies of the low temperature photolytic behavior of oxidized hydrogenase I from Clostridium pasteurianum

This publication has 27 references indexed in Scilit:

• The iron‐sulfur composition of the active site of hydrogenase from Desulfovibrio vulgaris (Hildenborough) deduced from its subunit structure and total iron‐sulfur content
  FEBS Letters, 1986
• Ligand binding to heme proteins: relevance of low-temperature data
  Biochemistry, 1986
• A reversible effect of low carbon monoxide concentrations on the EPR spectra of the periplasmic hydrogenase from Desulfovibriovulgaris
  Biochemical and Biophysical Research Communications, 1986
• EPR of a novel high‐spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough)
  FEBS Letters, 1986
• On the novel H2-activating iron-sulfur center of the “Fe-only” hydrogenases
  Biochimie, 1986
• Electron paramagnetic resonance and other properties of hydrogenases isolated from Desulfovibrio vulgaris (strain Hildenborough) and Megasphaera elsdenii
  European Journal of Biochemistry, 1983
• Low-temperature magnetic circular dichroism evidence for the conversion of four-iron-sulphur clusters in a ferredoxin from Clostridium pasteurianum into three-iron-sulphur clusters
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1981
• Hydrogenase
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1980
• Isolation and properties of a unidirectional H2-oxidizing hydrogenase from the strictly anaerobic N2-fixing bacterium Clostridium pasteurianum W5
  Biochemical and Biophysical Research Communications, 1978
• Separation of hydrogenase from intact cells of Desulfovibrio vulgaris Purification and properties
  FEBS Letters, 1978