Carboxylate Shifts in the Active Site of the Hydroxylase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath)

This publication has 26 references indexed in Scilit:

• Determining the Structure of a Hydroxylase Enzyme That Catalyzes the Conversion of Methane to Methanol in Methanotrophic Bacteria
  Accounts of Chemical Research, 1994
• Reactions of Non-Heme Iron(II) Centers with Dioxygen in Biology and Chemistry
  Chemical Reviews, 1994
• Spectroscopic studies of the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: comparison to deoxy and deoxy-azide hemerythrin
  Journal of the American Chemical Society, 1993
• Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2
  Journal of Molecular Biology, 1993
• Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath)
  Journal of Molecular Biology, 1992
• X-ray absorption, Moessbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase
  Journal of the American Chemical Society, 1991
• Structures of met and azidomet hemerythrin at 1·66 Å resolution
  Journal of Molecular Biology, 1991
• Structures of deoxy and oxy hemerythrin at 2.0 Å resolution
  Journal of Molecular Biology, 1991
• Oxo- and hydroxo-bridged diiron complexes: a chemical perspective on a biological unit
  Chemical Reviews, 1990
• Further characterisation of the FAD and Fe₂S₂ redox centres of component C, the NADH: acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
  European Journal of Biochemistry, 1985