Proton Transfer from Histidine 244 May Facilitate the 1,2 Rearrangement Reaction in Coenzyme B12-dependent Methylmalonyl-CoA Mutase

This publication has 32 references indexed in Scilit:

• Studies on the Catalysis of Carbon−Cobalt Bond Homolysis by Ribonucleoside Triphosphate Reductase: Evidence for Concerted Carbon−Cobalt Bond Homolysis and Thiyl Radical Formation^†
  Biochemistry, 1999
• Coupling of Cobalt−Carbon Bond Homolysis and Hydrogen Atom Abstraction in Adenosylcobalamin-Dependent Glutamate Mutase†
  Biochemistry, 1998
• STRUCTURE-BASED PERSPECTIVES ON B₁₂-DEPENDENT ENZYMES
  Annual Review of Biochemistry, 1997
• The Yin-Yang of cobalamin biochemistry
  Chemistry & Biology, 1997
• Evidence that Cobalt−Carbon Bond Homolysis is Coupled to Hydrogen Atom Abstraction from Substrate in Methylmalonyl-CoA Mutase†
  Biochemistry, 1997
• Evidence from Electron Paramagnetic Resonance Spectroscopy of the Participation of Radical Intermediates in the Reaction Catalyzed by Methylmalonyl-coenzyme A Mutase
  Journal of Biological Chemistry, 1995
• Electron Paramagnetic Resonance Studies of the Methylmalonyl‐CoA Mutase Reaction
  European Journal of Biochemistry, 1994
• The synthetic substrate succinyl(carbadethia)-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-CoA mutase
  Biochemical Journal, 1993
• Radical Intermediates in the Coenzyme B₁₂ Dependent Methylmalonyl‐CoA Mutase Reaction Shown by ESR Spectroscopy
  Angewandte Chemie International Edition in English, 1992
• Mechanisms of Coenzyme B ₁₂ -Dependent Rearrangements
  Science, 1985