Radical Catalysis in Coenzyme B12-Dependent Isomerization (Eliminating) Reactions (original) (raw)

articleJune 11, 2003

Radical Catalysis in Coenzyme B12-Dependent Isomerization (Eliminating) Reactions

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  2. Markus Ruetz, Romila Mascarenhas, Florian Widner, Christoph Kieninger, Markos Koutmos, Bernhard Kräutler, Ruma Banerjee. A Noble Metal Substitution Leads to B12 Cofactor Mimicry by a Rhodibalamin. Biochemistry 2024, 63 (15) , 1955-1962. https://doi.org/10.1021/acs.biochem.4c00216
  3. Alexandra Tsybizova, Lukas Fritsche, Larisa Miloglyadova, Bernhard Kräutler, Peter Chen. Cryogenic Ion Vibrational Predissociation (CIVP) Spectroscopy of Aryl Cobinamides in the Gas Phase: How Good Are the Calculations for Vitamin B12 Derivatives?. Journal of the American Chemical Society 2023, 145 (36) , 19561-19570. https://doi.org/10.1021/jacs.3c03001
  4. Wei Li, Meghan Kohne, Kurt Warncke. Reactivity Tracking of an Enzyme Progress Coordinate. The Journal of Physical Chemistry Letters 2023, 14 (32) , 7157-7164. https://doi.org/10.1021/acs.jpclett.3c01464
  5. Keita Shichijo, Yohei Kametani, Yoshihito Shiota, Kazunari Yoshizawa, Mamoru Fujitsuka, Hisashi Shimakoshi. Effect of Macrocycles on the Photochemical and Electrochemical Properties of Cobalt-Dehydrocorrin Complex: Formation and Investigation of Co(I) Species. Inorganic Chemistry 2023, 62 (30) , 11785-11795. https://doi.org/10.1021/acs.inorgchem.3c00882
  6. Yu-Hsuan Lee, Xueli Hou, Ridao Chen, Jianqiang Feng, Xiao Liu, Mark W. Ruszczycky, Jin-Ming Gao, Binju Wang, Jiahai Zhou, Hung-wen Liu. Radical S-Adenosyl Methionine Enzyme BlsE Catalyzes a Radical-Mediated 1,2-Diol Dehydration during the Biosynthesis of Blasticidin S. Journal of the American Chemical Society 2022, 144 (10) , 4478-4486. https://doi.org/10.1021/jacs.1c12010
  7. Oaikhena Zekeri Esezobor, Wenyi Zeng, Lukas Niederegger, Michael Grübel, Corinna R. Hess. Co–Mabiq Flies Solo: Light-Driven Markovnikov-Selective C- and N-Alkylation of Indoles and Indazoles without a Cocatalyst. Journal of the American Chemical Society 2022, 144 (7) , 2994-3004. https://doi.org/10.1021/jacs.1c10930
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  9. Aleksandra Potrząsaj, Mateusz Musiejuk, Wojciech Chaładaj, Maciej Giedyk, Dorota Gryko. Cobalt Catalyst Determines Regioselectivity in Ring Opening of Epoxides with Aryl Halides. Journal of the American Chemical Society 2021, 143 (25) , 9368-9376. https://doi.org/10.1021/jacs.1c00659
  10. Elvin V. Salerno, Nicholas A. Miller, Arkaprabha Konar, Yan Li, Christoph Kieninger, Bernhard Kräutler, Roseanne J. Sension. Ultrafast Excited State Dynamics and Fluorescence from Vitamin B12 and Organometallic [Co]–C≡C–R Cobalamins. The Journal of Physical Chemistry B 2020, 124 (30) , 6651-6656. https://doi.org/10.1021/acs.jpcb.0c04886
  11. Hao Yang, Stella Impano, Eric M. Shepard, Christopher D. James, William E. Broderick, Joan B. Broderick, Brian M. Hoffman. Photoinduced Electron Transfer in a Radical SAM Enzyme Generates an S-Adenosylmethionine Derived Methyl Radical. Journal of the American Chemical Society 2019, 141 (40) , 16117-16124. https://doi.org/10.1021/jacs.9b08541
  12. Meghan Kohne, Wei Li, Chen Zhu, Kurt Warncke. Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in B12-Dependent Ethanolamine Ammonia-Lyase. Biochemistry 2019, 58 (35) , 3683-3690. https://doi.org/10.1021/acs.biochem.9b00588
  13. Luka Bilić, Danijela Barić, Radha Dilip Banhatti, David M. Smith, Borislav Kovačević. Computational Study of Glycerol Binding within the Active Site of Coenzyme B12-Dependent Diol Dehydratase. The Journal of Physical Chemistry B 2019, 123 (29) , 6178-6187. https://doi.org/10.1021/acs.jpcb.9b04071
  14. Benjamen Nforneh, Kurt Warncke. Control of Solvent Dynamics around the B12-Dependent Ethanolamine Ammonia-Lyase Enzyme in Frozen Aqueous Solution by Using Dimethyl Sulfoxide Modulation of Mesodomain Volume. The Journal of Physical Chemistry B 2019, 123 (26) , 5395-5404. https://doi.org/10.1021/acs.jpcb.9b02239
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  16. Abdullah Al Mamun, Megan J. Toda, Piotr Lodowski, Pawel M. Kozlowski. Photolytic Cleavage of Co–C Bond in Coenzyme B12-Dependent Glutamate Mutase. The Journal of Physical Chemistry B 2019, 123 (12) , 2585-2598. https://doi.org/10.1021/acs.jpcb.8b07547
  17. Rubik Asatryan, Yudhajit Pal, Johannes Hachmann, Eli Ruckenstein. Roaming-like Mechanism for Dehydration of Diol Radicals. The Journal of Physical Chemistry A 2018, 122 (51) , 9738-9754. https://doi.org/10.1021/acs.jpca.8b08690
  18. Derek M. Gagnon, Troy A. Stich, Angad P. Mehta, Sameh H. Abdelwahed, Tadhg P. Begley, R. David Britt. An Aminoimidazole Radical Intermediate in the Anaerobic Biosynthesis of the 5,6-Dimethylbenzimidazole Ligand to Vitamin B12. Journal of the American Chemical Society 2018, 140 (40) , 12798-12807. https://doi.org/10.1021/jacs.8b05686
  19. Abdullah Al Mamun, Megan J. Toda, Piotr Lodowski, Maria Jaworska, Pawel M. Kozlowski. Mechanism of Light Induced Radical Pair Formation in Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase. ACS Catalysis 2018, 8 (8) , 7164-7178. https://doi.org/10.1021/acscatal.8b00120
  20. Borislav Kovačević, Danijela Barić, Darko Babić, Luka Bilić, Marko Hanževački, Gregory M. Sandala, Leo Radom, David M. Smith. Computational Tale of Two Enzymes: Glycerol Dehydration With or Without B12. Journal of the American Chemical Society 2018, 140 (27) , 8487-8496. https://doi.org/10.1021/jacs.8b03109
  21. Yeonjin Ko, Geng-Min Lin, Mark W. Ruszczycky, Hung-wen Liu. Mechanistic Implications of the Deamination of TDP-4-amino-4-deoxy-d-fucose Catalyzed by the Radical SAM Enzyme DesII. Biochemistry 2018, 57 (22) , 3130-3133. https://doi.org/10.1021/acs.biochem.8b00110
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  23. Wan-Qiu Liu, Patricia Amara, Jean-Marie Mouesca, Xinjian Ji, Oriane Renoux, Lydie Martin, Chen Zhang, Qi Zhang, and Yvain Nicolet . 1,2-Diol Dehydration by the Radical SAM Enzyme AprD4: A Matter of Proton Circulation and Substrate Flexibility. Journal of the American Chemical Society 2018, 140 (4) , 1365-1371. https://doi.org/10.1021/jacs.7b10501
  24. Fabio Parmeggiani, Nicholas J. Weise, Syed T. Ahmed, and Nicholas J. Turner . Synthetic and Therapeutic Applications of Ammonia-lyases and Aminomutases. Chemical Reviews 2018, 118 (1) , 73-118. https://doi.org/10.1021/acs.chemrev.6b00824
  25. Benjamen Nforneh and Kurt Warncke . Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200–265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide. The Journal of Physical Chemistry B 2017, 121 (49) , 11109-11118. https://doi.org/10.1021/acs.jpcb.7b09711
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  28. Tetsuo Toraya, Aya Tanokuchi, Ai Yamasaki, Takehiro Nakamura, Kenichi Ogura, and Takamasa Tobimatsu . Diol Dehydratase-Reactivase Is Essential for Recycling of Coenzyme B12 in Diol Dehydratase. Biochemistry 2016, 55 (1) , 69-78. https://doi.org/10.1021/acs.biochem.5b01023
  29. Masaki Horitani, Amanda S. Byer, Krista A. Shisler, Tilak Chandra, Joan B. Broderick, and Brian M. Hoffman . Why Nature Uses Radical SAM Enzymes so Widely: Electron Nuclear Double Resonance Studies of Lysine 2,3-Aminomutase Show the 5′-dAdo• “Free Radical” Is Never Free. Journal of the American Chemical Society 2015, 137 (22) , 7111-7121. https://doi.org/10.1021/jacs.5b00498
  30. Hartmut Herrmann, Thomas Schaefer, Andreas Tilgner, Sarah A. Styler, Christian Weller, Monique Teich, and Tobias Otto . Tropospheric Aqueous-Phase Chemistry: Kinetics, Mechanisms, and Its Coupling to a Changing Gas Phase. Chemical Reviews 2015, 115 (10) , 4259-4334. https://doi.org/10.1021/cr500447k
  31. Amarendra Nath Maity, Hsin-Hua Lin, Hsiang-Sheng Chiang, Hsin-Hsi Lo, and Shyue-Chu Ke . Reaction of Pyridoxal-5′-phosphate-N-oxide with Lysine 5,6-Aminomutase: Enzyme Flexibility toward Cofactor Analog. ACS Catalysis 2015, 5 (5) , 3093-3099. https://doi.org/10.1021/acscatal.5b00671
  32. Geng-Min Lin, Sei-Hyun Choi, Mark W. Ruszczycky, and Hung-wen Liu . Mechanistic Investigation of the Radical S-Adenosyl-l-methionine Enzyme DesII Using Fluorinated Analogues. Journal of the American Chemical Society 2015, 137 (15) , 4964-4967. https://doi.org/10.1021/jacs.5b02545
  33. Karen S. Conrad, Christopher D. Jordan, Kenneth L. Brown, and Thomas C. Brunold . Spectroscopic and Computational Studies of Cobalamin Species with Variable Lower Axial Ligation: Implications for the Mechanism of Co–C Bond Activation by Class I Cobalamin-Dependent Isomerases. Inorganic Chemistry 2015, 54 (8) , 3736-3747. https://doi.org/10.1021/ic502665x
  34. Piotr Lodowski, Maria Jaworska, Tadeusz Andruniów, Brady D. Garabato, and Pawel M. Kozlowski . Mechanism of Co–C Bond Photolysis in the Base-On Form of Methylcobalamin. The Journal of Physical Chemistry A 2014, 118 (50) , 11718-11734. https://doi.org/10.1021/jp508513p
  35. Koichi Mori, Toshihiro Oiwa, Satoshi Kawaguchi, Kyosuke Kondo, Yusuke Takahashi, and Tetsuo Toraya . Catalytic Roles of Substrate-Binding Residues in Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase. Biochemistry 2014, 53 (16) , 2661-2671. https://doi.org/10.1021/bi500223k
  36. Gabriel D. Román-Meléndez, Patrick von Glehn, Jeremy N. Harvey, Adrian J. Mulholland, and E. Neil G. Marsh . Role of Active Site Residues in Promoting Cobalt–Carbon Bond Homolysis in Adenosylcobalamin-Dependent Mutases Revealed through Experiment and Computation. Biochemistry 2014, 53 (1) , 169-177. https://doi.org/10.1021/bi4012644
  37. Koichi Mori, Koji Obayashi, Yasuhiro Hosokawa, Akina Yamamoto, Mayumi Yano, Toshiyuki Yoshinaga, and Tetsuo Toraya . Essential Roles of Nucleotide-Switch and Metal-Coordinating Residues for Chaperone Function of Diol Dehydratase-Reactivase. Biochemistry 2013, 52 (48) , 8677-8686. https://doi.org/10.1021/bi401290j
  38. Miao Wang and Kurt Warncke . Entropic Origin of Cobalt–Carbon Bond Cleavage Catalysis in Adenosylcobalamin-Dependent Ethanolamine Ammonia-Lyase. Journal of the American Chemical Society 2013, 135 (40) , 15077-15084. https://doi.org/10.1021/ja404467d
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  40. Caitlyn Makins, Alex V. Pickering, Chloe Mariani, and Kirsten R. Wolthers . Mutagenesis of a Conserved Glutamate Reveals the Contribution of Electrostatic Energy to Adenosylcobalamin Co–C Bond Homolysis in Ornithine 4,5-Aminomutase and Methylmalonyl-CoA Mutase. Biochemistry 2013, 52 (5) , 878-888. https://doi.org/10.1021/bi3012719
  41. Yung-Han Chen, Amarendra N. Maity, Perry A. Frey, and Shyue-Chu Ke . Mechanism-based Inhibition Reveals Transitions between Two Conformational States in the Action of Lysine 5,6-Aminomutase: A Combination of Electron Paramagnetic Resonance Spectroscopy, Electron Nuclear Double Resonance Spectroscopy, and Density Functional Theory Study. Journal of the American Chemical Society 2013, 135 (2) , 788-794. https://doi.org/10.1021/ja309603a
  42. Kazuki Doitomi, Takashi Kamachi, Tetsuo Toraya, and Kazunari Yoshizawa . Inactivation Mechanism of Glycerol Dehydration by Diol Dehydratase from Combined Quantum Mechanical/Molecular Mechanical Calculations. Biochemistry 2012, 51 (45) , 9202-9210. https://doi.org/10.1021/bi300488u
  43. Valentin Cracan and Ruma Banerjee . Novel B12-Dependent Acyl-CoA Mutases and Their Biotechnological Potential. Biochemistry 2012, 51 (31) , 6039-6046. https://doi.org/10.1021/bi300827v
  44. Mikolaj Feliks and G. Matthias Ullmann . Glycerol Dehydratation by the B12-Independent Enzyme May Not Involve the Migration of a Hydroxyl Group: A Computational Study. The Journal of Physical Chemistry B 2012, 116 (24) , 7076-7087. https://doi.org/10.1021/jp301165b
  45. Alex R. Jones, Henry J. Russell, Gregory M. Greetham, Michael Towrie, Sam Hay, and Nigel S. Scrutton . Ultrafast Infrared Spectral Fingerprints of Vitamin B12 and Related Cobalamins. The Journal of Physical Chemistry A 2012, 116 (23) , 5586-5594. https://doi.org/10.1021/jp304594d
  46. Pawel M. Kozlowski and Manoj Kumar , Piotr Piecuch, Wei Li, Nicholas P. Bauman, and Jared A. Hansen , Piotr Lodowski and Maria Jaworska . The Cobalt–Methyl Bond Dissociation in Methylcobalamin: New Benchmark Analysis Based on Density Functional Theory and Completely Renormalized Coupled-Cluster Calculations. Journal of Chemical Theory and Computation 2012, 8 (6) , 1870-1894. https://doi.org/10.1021/ct300170y
  47. Neeraj Kumar, Shubin Liu, and Pawel M. Kozlowski . Charge Separation Propensity of the Coenzyme B12–Tyrosine Complex in Adenosylcobalamin-Dependent Methylmalonyl–CoA Mutase Enzyme. The Journal of Physical Chemistry Letters 2012, 3 (8) , 1035-1038. https://doi.org/10.1021/jz300102s
  48. Jiayun Pang, Xin Li, Keiji Morokuma, Nigel S. Scrutton, and Michael J. Sutcliffe . Large-Scale Domain Conformational Change Is Coupled to the Activation of the Co–C Bond in the B12-Dependent Enzyme Ornithine 4,5-Aminomutase: A Computational Study. Journal of the American Chemical Society 2012, 134 (4) , 2367-2377. https://doi.org/10.1021/ja210417k
  49. Piotr Lodowski, Maria Jaworska, Karina Kornobis, Tadeusz Andruniów, and Pawel M. Kozlowski . Electronic and Structural Properties of Low-lying Excited States of Vitamin B12. The Journal of Physical Chemistry B 2011, 115 (45) , 13304-13319. https://doi.org/10.1021/jp200911y
  50. Yung-Han Chen, Amarendra N. Maity, Yu-Chiang Pan, Perry A. Frey, and Shyue-Chu Ke . Radical Stabilization Is Crucial in the Mechanism of Action of Lysine 5,6-Aminomutase: Role of Tyrosine-263α As Revealed by Electron Paramagnetic Resonance Spectroscopy. Journal of the American Chemical Society 2011, 133 (43) , 17152-17155. https://doi.org/10.1021/ja207766c
  51. Sean A. Newmister, Michele M. Otte, Jorge C. Escalante-Semerena, and Ivan Rayment . Structure and Mutational Analysis of the Archaeal GTP:AdoCbi-P Guanylyltransferase (CobY) from Methanocaldococcus jannaschii: Insights into GTP Binding and Dimerization. Biochemistry 2011, 50 (23) , 5301-5313. https://doi.org/10.1021/bi200329t
  52. Mark W. Ruszczycky, Sei-hyun Choi, Steven O. Mansoorabadi, and Hung-wen Liu . Mechanistic Studies of the Radical S-Adenosyl-l-methionine Enzyme DesII: EPR Characterization of a Radical Intermediate Generated During Its Catalyzed Dehydrogenation of TDP-d-Quinovose. Journal of the American Chemical Society 2011, 133 (19) , 7292-7295. https://doi.org/10.1021/ja201212f
  53. Wesley D. Robertson, Miao Wang, and Kurt Warncke . Characterization of Protein Contributions to Cobalt−Carbon Bond Cleavage Catalysis in Adenosylcobalamin-Dependent Ethanolamine Ammonia-Lyase by using Photolysis in the Ternary Complex. Journal of the American Chemical Society 2011, 133 (18) , 6968-6977. https://doi.org/10.1021/ja107052p
  54. Takashi Kamachi, Kazuki Doitomi, Masanori Takahata, Tetsuo Toraya, and Kazunari Yoshizawa . Catalytic Roles of the Metal Ion in the Substrate-Binding Site of Coenzyme B12-Dependent Diol Dehydratase. Inorganic Chemistry 2011, 50 (7) , 2944-2952. https://doi.org/10.1021/ic102352b
  55. Xiao-Lei Wang and Jun-Min Quan . Intermediate-Assisted Multifunctional Catalysis in the Conversion of Flavin to 5,6-Dimethylbenzimidazole by BluB: A Density Functional Theory Study. Journal of the American Chemical Society 2011, 133 (11) , 4079-4091. https://doi.org/10.1021/ja1106207
  56. Naoki Shibata, Yoshiki Higuchi, and Tetsuo Toraya . How Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase Deals with Both Enantiomers of 2-Amino-1-propanol as Substrates: Structure-Based Rationalization,,. Biochemistry 2011, 50 (4) , 591-598. https://doi.org/10.1021/bi101696h
  57. Karl-Magnus Larsson, Derek T. Logan, and Pär Nordlund . Structural Basis for Adenosylcobalamin Activation in AdoCbl-Dependent Ribonucleotide Reductases. ACS Chemical Biology 2010, 5 (10) , 933-942. https://doi.org/10.1021/cb1000845
  58. Mercedes Alfonso-Prieto, Xevi Biarnés, Manoj Kumar, Carme Rovira, and Pawel M. Kozlowski . Reductive Cleavage Mechanism of Co−C Bond in Cobalamin-Dependent Methionine Synthase. The Journal of Physical Chemistry B 2010, 114 (40) , 12965-12971. https://doi.org/10.1021/jp1043738
  59. Sabine Vollenweider, Stefan Evers, Karin Zurbriggen, and Christophe Lacroix . Unraveling the Hydroxypropionaldehyde (HPA) System: An Active Antimicrobial Agent against Human Pathogens. Journal of Agricultural and Food Chemistry 2010, 58 (19) , 10315-10322. https://doi.org/10.1021/jf1010897
  60. Tetsuo Toraya, Susumu Honda and Koichi Mori . Coenzyme B12-Dependent Diol Dehydratase Is a Potassium Ion-Requiring Calcium Metalloenzyme: Evidence That the Substrate-Coordinated Metal Ion Is Calcium. Biochemistry 2010, 49 (33) , 7210-7217. https://doi.org/10.1021/bi100561m
  61. Chen Zhu and Kurt Warncke. Kinetic Isolation and Characterization of the Radical Rearrangement Step in Coenzyme B12-Dependent Ethanolamine Ammonia-lyase. Journal of the American Chemical Society 2010, 132 (28) , 9610-9615. https://doi.org/10.1021/ja907769g
  62. Pawel M. Kozlowski, Takashi Kamachi, Manoj Kumar, Tomonori Nakayama and Kazunari Yoshizawa . Theoretical Analysis of the Diradical Nature of Adenosylcobalamin Cofactor−Tyrosine Complex in B12-Dependent Mutases: Inspiring PCET-Driven Enzymatic Catalysis. The Journal of Physical Chemistry B 2010, 114 (17) , 5928-5939. https://doi.org/10.1021/jp100573b
  63. Mark W. Ruszczycky, Sei-hyun Choi and Hung-wen Liu. Stoichiometry of the Redox Neutral Deamination and Oxidative Dehydrogenation Reactions Catalyzed by the Radical SAM Enzyme DesII. Journal of the American Chemical Society 2010, 132 (7) , 2359-2369. https://doi.org/10.1021/ja909451a
  64. Israel Fernández, Fernando P. Cossío and Miguel A. Sierra. Dyotropic Reactions: Mechanisms and Synthetic Applications. Chemical Reviews 2009, 109 (12) , 6687-6711. https://doi.org/10.1021/cr900209c
  65. Alex R. Jones, Jonathan R. Woodward and Nigel S. Scrutton. Continuous Wave Photolysis Magnetic Field Effect Investigations with Free and Protein-Bound Alkylcobalamins. Journal of the American Chemical Society 2009, 131 (47) , 17246-17253. https://doi.org/10.1021/ja9059238
  66. Jadwiga Kuta, Jochen Wuerges, Lucio Randaccio and Pawel M. Kozlowski . Axial Bonding in Alkylcobalamins: DFT Analysis of the Inverse Versus Normal Trans Influence. The Journal of Physical Chemistry A 2009, 113 (43) , 11604-11612. https://doi.org/10.1021/jp901397p
  67. Mark S. Taylor, Sandra A. Ivanic, Geoffrey P. F. Wood, Christopher J. Easton, George B. Bacskay and Leo Radom. Hydrogen Abstraction by Chlorine Atom from Small Organic Molecules Containing Amino Acid Functionalities: An Assessment of Theoretical Procedures. The Journal of Physical Chemistry A 2009, 113 (43) , 11817-11832. https://doi.org/10.1021/jp9029437
  68. Amarendra N. Maity, Chih-Pin Hsieh, Ming-Hui Huang, Yung-Han Chen, Kuo-Hsiang Tang, Elham Behshad, Perry A. Frey and Shyue-Chu Ke . Evidence for Conformational Movement and Radical Mechanism in the Reaction of 4-Thia-l-lysine with Lysine 5,6-Aminomutase. The Journal of Physical Chemistry B 2009, 113 (36) , 12161-12163. https://doi.org/10.1021/jp905357a
  69. Kuo-Hsiang Tang, Steven O. Mansoorabadi, George H. Reed and Perry A. Frey. Radical Triplets and Suicide Inhibition in Reactions of 4-Thia-d- and 4-Thia-l-lysine with Lysine 5,6-Aminomutase. Biochemistry 2009, 48 (34) , 8151-8160. https://doi.org/10.1021/bi900828f
  70. Manoj Kumar and Pawel M. Kozlowski. Role of Tyrosine Residue in the Activation of Co−C Bond in Coenzyme B12-Dependent Enzymes: Another Case of Proton-Coupled Electron Transfer?. The Journal of Physical Chemistry B 2009, 113 (27) , 9050-9054. https://doi.org/10.1021/jp903878y
  71. Takashi Kamachi, Masanori Takahata, Tetsuo Toraya and Kazunari Yoshizawa . What is the Identity of the Metal Ions in the Active Sites of Coenzyme B12-Dependent Diol Dehydratase? A Computational Mutation Analysis. The Journal of Physical Chemistry B 2009, 113 (25) , 8435-8438. https://doi.org/10.1021/jp9001737
  72. Piotr Lodowski, Maria Jaworska, Tadeusz Andruniów, Manoj Kumar and Pawel M. Kozlowski . Photodissociation of Co−C Bond in Methyl- and Ethylcobalamin: An Insight from TD-DFT Calculations. The Journal of Physical Chemistry B 2009, 113 (19) , 6898-6909. https://doi.org/10.1021/jp810223h
  73. Xin Li, Lung Wa Chung, Piotr Paneth and Keiji Morokuma . DFT and ONIOM(DFT:MM) Studies on Co−C Bond Cleavage and Hydrogen Transfer in B12-Dependent Methylmalonyl-CoA Mutase. Stepwise or Concerted Mechanism?. Journal of the American Chemical Society 2009, 131 (14) , 5115-5125. https://doi.org/10.1021/ja807677z
  74. Wesley D. Robertson and Kurt Warncke. Photolysis of Adenosylcobalamin and Radical Pair Recombination in Ethanolamine Ammonia-Lyase Probed on the Micro- to Millisecond Time Scale by Using Time-Resolved Optical Absorption Spectroscopy. Biochemistry 2009, 48 (1) , 140-147. https://doi.org/10.1021/bi801659e
  75. Li Sun, Olivia A. Groover, Jeffrey M. Canfield and Kurt Warncke. Critical Role of Arginine 160 of the EutB Protein Subunit for Active Site Structure and Radical Catalysis in Coenzyme B12-Dependent Ethanolamine Ammonia-lyase. Biochemistry 2008, 47 (20) , 5523-5535. https://doi.org/10.1021/bi702366e
  76. Miao Wang and, Kurt Warncke. Kinetic and Thermodynamic Characterization of CoII−Substrate Radical Pair Formation in Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase in a Cryosolvent System by Using Time-Resolved, Full-Spectrum Continuous-Wave Electron Paramagnetic Resonance Spectroscopy. Journal of the American Chemical Society 2008, 130 (14) , 4846-4858. https://doi.org/10.1021/ja710069y
  77. Koichiro Kinoshita, Masahiro Kawata, Ken-ichi Ogura, Ai Yamasaki, Takeshi Watanabe, Noriaki Komoto, Naoki Hieda, Mamoru Yamanishi, Takamasa Tobimatsu and Tetsuo Toraya. Histidine-α143 Assists 1,2-Hydroxyl Group Migration and Protects Radical Intermediates in Coenzyme B12-Dependent Diol Dehydratase. Biochemistry 2008, 47 (10) , 3162-3173. https://doi.org/10.1021/bi7018095
  78. Wlodzimierz Galezowski,, Jadwiga Kuta, and, Pawel M. Kozlowski. DFT Study of Co−C Bond Cleavage in the Neutral and One-Electron-Reduced Alkyl−Cobalt(III) Phthalocyanines. The Journal of Physical Chemistry B 2008, 112 (10) , 3177-3183. https://doi.org/10.1021/jp0769678
  79. Alex R. Jones,, Sam Hay,, Jonathan R. Woodward, and, Nigel S. Scrutton. Magnetic Field Effect Studies Indicate Reduced Geminate Recombination of the Radical Pair in Substrate-Bound Adenosylcobalamin-Dependent Ethanolamine Ammonia Lyase. Journal of the American Chemical Society 2007, 129 (50) , 15718-15727. https://doi.org/10.1021/ja077124x
  80. Carme Rovira and, Pawel M. Kozlowski. First Principles Study of Coenzyme B12. Crystal Packing Forces Effect on Axial Bond Lengths. The Journal of Physical Chemistry B 2007, 111 (12) , 3251-3257. https://doi.org/10.1021/jp0660029
  81. Gregory M. Sandala,, David M. Smith,, E. Neil G. Marsh, and, Leo Radom. Toward an Improved Understanding of the Glutamate Mutase System. Journal of the American Chemical Society 2007, 129 (6) , 1623-1633. https://doi.org/10.1021/ja066432c
  82. Steven O. Mansoorabadi,, Olafur Th. Magnusson,, Russell R. Poyner,, Perry A. Frey, and, George H. Reed. Analysis of the Cob(II)alamin−5‘-Deoxy-3‘,4‘-anhydroadenosyl Radical Triplet Spin System in the Active Site of Diol Dehydrase. Biochemistry 2006, 45 (48) , 14362-14370. https://doi.org/10.1021/bi061586q
  83. Perry A. Frey,, Adrian D. Hegeman, and, George H. Reed. Free Radical Mechanisms in Enzymology. Chemical Reviews 2006, 106 (8) , 3302-3316. https://doi.org/10.1021/cr050292s
  84. Stephen W. Ragsdale. Metals and Their Scaffolds To Promote Difficult Enzymatic Reactions. Chemical Reviews 2006, 106 (8) , 3317-3337. https://doi.org/10.1021/cr0503153
  85. Pawel M. Kozlowski,, Tadeusz Andruniow,, Andrzej A. Jarzecki,, Marek Z. Zgierski, and, Thomas G. Spiro. DFT Analysis of Co−Alkyl and Co−Adenosyl Vibrational Modes in B12-Cofactors. Inorganic Chemistry 2006, 45 (14) , 5585-5590. https://doi.org/10.1021/ic052069j
  86. Russell R. Poyner,, Mark A. Anderson,, Vahe Bandarian,, W. Wallace Cleland, and, George H. Reed. Probing Nitrogen-Sensitive Steps in the Free-Radical-Mediated Deamination of Amino Alcohols by Ethanolamine Ammonia-Lyase. Journal of the American Chemical Society 2006, 128 (22) , 7120-7121. https://doi.org/10.1021/ja060710q
  87. Amanda J. Brooks,, Christel C. Fox,, E. Neil G. Marsh,, Monica Vlasie,, Ruma Banerjee, and, Thomas C. Brunold. Electronic Structure Studies of the Adenosylcobalamin Cofactor in Glutamate Mutase. Biochemistry 2005, 44 (46) , 15167-15181. https://doi.org/10.1021/bi051094y
  88. Libin Xu and, Martin Newcomb. Acid-, Base-, and Lewis-Acid-Catalyzed Heterolysis of Methoxide from an α-Hydroxy-β-methoxy Radical: Models for Reactions Catalyzed by Coenzyme B12-Dependent Diol Dehydratase. The Journal of Organic Chemistry 2005, 70 (23) , 9296-9303. https://doi.org/10.1021/jo051349d
  89. Roseanne J. Sension,, D. Ahmasi Harris,, Andrew Stickrath,, Allwyn G. Cole,, Christel C. Fox, and, E. Neil G. Marsh. Time-Resolved Measurements of the Photolysis and Recombination of Adenosylcobalamin Bound to Glutamate Mutase. The Journal of Physical Chemistry B 2005, 109 (38) , 18146-18152. https://doi.org/10.1021/jp052492d
  90. Siu Kwan Yeung and, Kin Shing Chan. 1,2-Rearrangements of β-Nitrogen-Substituted (Porphyrinato)rhodium(III) Ethyls. Organometallics 2005, 24 (11) , 2561-2563. https://doi.org/10.1021/om0501475
  91. Kurt Warncke. Characterization of the Product Radical Structure in the CoII-Product Radical Pair State of Coenzyme B12-Dependent Ethanolamine Deaminase by Using Three-Pulse 2H ESEEM Spectroscopy. Biochemistry 2005, 44 (9) , 3184-3193. https://doi.org/10.1021/bi048196t
  92. Mamoru Yamanishi,, Hirofumi Ide,, Yoshitake Murakami, and, Tetsuo Toraya. Identification of the 1,2-Propanediol-1-yl Radical as an Intermediate in Adenosylcobalamin-Dependent Diol Dehydratase Reaction. Biochemistry 2005, 44 (6) , 2113-2118. https://doi.org/10.1021/bi0481850
  93. Takashi Kamachi,, Tetsuo Toraya, and, Kazunari Yoshizawa. Catalytic Roles of Active-Site Amino Acid Residues of Coenzyme B12-Dependent Diol Dehydratase: Protonation State of Histidine and Pull Effect of Glutamate. Journal of the American Chemical Society 2004, 126 (49) , 16207-16216. https://doi.org/10.1021/ja045572o
  94. Neil Miranda,, Libin Xu, and, Martin Newcomb. Lewis Acid Catalysis in Heterolysis Reactions of Glycol Ether Radicals Mimicking Diol Dehydratase-Catalyzed Reactions. Organic Letters 2004, 6 (24) , 4511-4514. https://doi.org/10.1021/ol0481131
  95. Pawel M. Kozlowski and, Marek Z. Zgierski. Electronic and Steric Influence of Trans Axial Base on the Stereoelectronic Properties of Cobalamins. The Journal of Physical Chemistry B 2004, 108 (37) , 14163-14170. https://doi.org/10.1021/jp040373c
  96. Kurt Warncke and, Jeffrey M. Canfield. Direct Determination of Product Radical Structure Reveals the Radical Rearrangement Pathway in a Coenzyme B12-Dependent Enzyme. Journal of the American Chemical Society 2004, 126 (19) , 5930-5931. https://doi.org/10.1021/ja031569d
  97. Yu Lin, Long Jiang, Yupeng Wan, Yunfei Li, Hao Lan, Chao Xu, Mo Xian. Controllable Enhanced Reactivity of Radical Intermediates in Olefin Cyclopropanation via Electron‐Withdrawing Substituents in Biomimetic Catalysts. Chinese Journal of Chemistry 2026, 44 (6) , 813-820. https://doi.org/10.1002/cjoc.70409
  98. Florian J. Widner, Naziyat I. Khan, Evelyne Deery, Martin J. Warren, Michiko E. Taga, Bernhard Kräutler. Repression of bacterial gene expression by antivitamin B 12 binding to a cobalamin riboswitch. RSC Chemical Biology 2026, 7 (3) , 498-504. https://doi.org/10.1039/D5CB00308C
  99. Chae Yeong Na, Abdul Nasir, Raeyun Park, Young Joo Yeon, Seung-Ho Baek, Sunghoon Park, Ye Seop Park, Min-Duk Seo, Tae Hyeon Yoo. Engineering the α- and β-subunit interface of a coenzyme B12-dependent glycerol dehydratase for enhancing its resistance to inactivation. Bioresource Technology 2026, 442 , 133733. https://doi.org/10.1016/j.biortech.2025.133733
  100. Naoki Hieda, Reiko Bando, Keisuke Maeda, Koichi Mori, Tetsuo Toraya. Mechanism for reactivation of inactivated holoenzymes of coenzyme B 12 ‐dependent ethanolamine ammonia‐lyase by the reactivating chaperone EutA. The FEBS Journal 2026, 293 (2) , 532-548. https://doi.org/10.1111/febs.70254

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