Sulfite Reductase (NADPH)

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  Subject Areas on Research

  • 57Fe and 1H electron-nuclear double resonance of three doubly reduced states Escherichia coli sulfite reductase. 
  • Activated conformers of Escherichia coli sulfite reductase heme protein subunit. 
  • Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite. 
  • Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase. 
  • Electron paramagnetic resonance and optical evidence for interaction between siroheme and Fe4S4 prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands. 
  • High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. 
  • Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. 
  • Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. 
  • The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase.