Radical peregrinations catalyzed by coenzyme B12-dependent enzymes

[1] Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B12 [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 370 (01) : 138 - 141

[2] BABIOR BM, 1974, J BIOL CHEM, V249, P4537

[3] Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: Determination of the number of exchangeable hydrogens in the enzyme-cofactor complex [J]. BIOCHEMISTRY, 2000, 39 (39) : 12069 - 12075

[4] EVIDENCE FOR A MECHANISM INVOLVING TRANSIENT FRAGMENTATION IN CARBON SKELETON REARRANGEMENTS DEPENDENT ON COENZYME B-12 [J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 1995, 34 (21) : 2398 - 2401

[5] INTERPRETATION OF ELECTRON-SPIN RESONANCE-SPECTRA DUE TO SOME B12-DEPENDENT ENZYME-REACTIONS [J]. JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS II, 1978, 74 : 417 - 431

[6] COENZYME-B-12 DEPENDENT RIBONUCLEOTIDE REDUCTASE - EVIDENCE FOR THE PARTICIPATION OF 5 CYSTEINE RESIDUES IN RIBONUCLEOTIDE REDUCTION [J]. BIOCHEMISTRY, 1994, 33 (42) : 12676 - 12685

[7] Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium [J]. BIOCHEMISTRY, 1998, 37 (12) : 4105 - 4113

[8] EFFECTS OF AXIAL LIGATION ON THE THERMOLYSIS OF BENZYLCOBAMIDES AND NEOPENTYLCOBAMIDES - ANALYSIS OF THE BASE-ON EFFECT [J]. INORGANIC CHEMISTRY, 1991, 30 (18) : 3420 - 3430

[9] Activation parameters for the carbon-cobalt bond homolysis of coenzyme B12 induced by the B12-dependent ribonucleotide reductase from Lactobacillus leichmannii [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (37) : 9466 - 9474

[10] Thermolysis of coenzymes B12 at physiological temperatures:: activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii [J]. JOURNAL OF INORGANIC BIOCHEMISTRY, 1999, 77 (3-4) : 185 - 195

[1] Ethanolamine ammonia-lyase has a "base-on" binding mode for coenzyme B12 [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 370 (01) : 138 - 141

[2] BABIOR BM, 1974, J BIOL CHEM, V249, P4537

[3] Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: Determination of the number of exchangeable hydrogens in the enzyme-cofactor complex [J]. BIOCHEMISTRY, 2000, 39 (39) : 12069 - 12075

[4] EVIDENCE FOR A MECHANISM INVOLVING TRANSIENT FRAGMENTATION IN CARBON SKELETON REARRANGEMENTS DEPENDENT ON COENZYME B-12 [J]. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 1995, 34 (21) : 2398 - 2401

[5] INTERPRETATION OF ELECTRON-SPIN RESONANCE-SPECTRA DUE TO SOME B12-DEPENDENT ENZYME-REACTIONS [J]. JOURNAL OF THE CHEMICAL SOCIETY-FARADAY TRANSACTIONS II, 1978, 74 : 417 - 431

[6] COENZYME-B-12 DEPENDENT RIBONUCLEOTIDE REDUCTASE - EVIDENCE FOR THE PARTICIPATION OF 5 CYSTEINE RESIDUES IN RIBONUCLEOTIDE REDUCTION [J]. BIOCHEMISTRY, 1994, 33 (42) : 12676 - 12685

[7] Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium [J]. BIOCHEMISTRY, 1998, 37 (12) : 4105 - 4113

[8] EFFECTS OF AXIAL LIGATION ON THE THERMOLYSIS OF BENZYLCOBAMIDES AND NEOPENTYLCOBAMIDES - ANALYSIS OF THE BASE-ON EFFECT [J]. INORGANIC CHEMISTRY, 1991, 30 (18) : 3420 - 3430

[9] Activation parameters for the carbon-cobalt bond homolysis of coenzyme B12 induced by the B12-dependent ribonucleotide reductase from Lactobacillus leichmannii [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (37) : 9466 - 9474

[10] Thermolysis of coenzymes B12 at physiological temperatures:: activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii [J]. JOURNAL OF INORGANIC BIOCHEMISTRY, 1999, 77 (3-4) : 185 - 195