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Facilitation of Enzyme-Catalyzed Reactions by Partial Proton Transfer:  Application to Coenzyme-B12-Dependent Methylmalonyl-CoA Mutase

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    Facilitation of Enzyme-Catalyzed Reactions by Partial Proton Transfer:  Application to Coenzyme-B12-Dependent Methylmalonyl-CoA Mutase
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    Research School of Chemistry Australian National University Canberra, ACT 0200, Australia Department of Chemistry, University of Newcastle upon Tyne Newcastle upon Tyne, NE1 7RU, U.K.
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 1999, 121, 6, 1383–1384
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    https://doi.org/10.1021/ja983512a
    Published January 30, 1999
    Copyright © 1999 American Chemical Society
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    Copyright © 1999 American Chemical Society

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    †

     Australian National University.

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     University of Newcastle upon Tyne.

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    This article is cited by 38 publications.

    1. Phillip P. Painter, Bonnie M. Wong, and Dean J. Tantillo . Facilitating the Cope Rearrangement by Partial Protonation: Implications for Synthesis and Biosynthesis. Organic Letters 2014, 16 (18) , 4818-4821. https://doi.org/10.1021/ol5023036
    2. Judith B. Rommel and Johannes Kästner . The Fragmentation–Recombination Mechanism of the Enzyme Glutamate Mutase Studied by QM/MM Simulations. Journal of the American Chemical Society 2011, 133 (26) , 10195-10203. https://doi.org/10.1021/ja202312d
    3. Gregory M. Sandala, David M. Smith and Leo Radom . Modeling the Reactions Catalyzed by Coenzyme B12-Dependent Enzymes. Accounts of Chemical Research 2010, 43 (5) , 642-651. https://doi.org/10.1021/ar900260c
    4. Fu-Qiang Shi,, Xin Li,, Yuanzhi Xia,, Liming Zhang, and, Zhi-Xiang Yu. DFT Study of the Mechanisms of In Water Au(I)-Catalyzed Tandem [3,3]-Rearrangement/Nazarov Reaction/[1,2]-Hydrogen Shift of Enynyl Acetates:  A Proton-Transport Catalysis Strategy in the Water-Catalyzed [1,2]-Hydrogen Shift. Journal of the American Chemical Society 2007, 129 (50) , 15503-15512. https://doi.org/10.1021/ja071070+
    5. Dominique Padovani and, Ruma Banerjee. Alternative Pathways for Radical Dissipation in an Active Site Mutant of B12-Dependent Methylmalonyl-CoA Mutase. Biochemistry 2006, 45 (9) , 2951-2959. https://doi.org/10.1021/bi051742d
    6. Monica D. Vlasie and, Ruma Banerjee. When a Spectator Turns Killer:  Suicidal Electron Transfer from Cobalamin in Methylmalonyl-CoA Mutase. Biochemistry 2004, 43 (26) , 8410-8417. https://doi.org/10.1021/bi036299q
    7. Marija Semialjac and, Helmut Schwarz. Computational Study on Mechanistic Details of the Aminoethanol Rearrangement Catalyzed by the Vitamin B12-Dependent Ethanolamine Ammonia Lyase:  His and Asp/Glu Acting Simultaneously as Catalytic Auxiliaries. The Journal of Organic Chemistry 2003, 68 (18) , 6967-6983. https://doi.org/10.1021/jo0301705
    8. Fahmi Himo and, Per E. M. Siegbahn. Quantum Chemical Studies of Radical-Containing Enzymes. Chemical Reviews 2003, 103 (6) , 2421-2456. https://doi.org/10.1021/cr020436s
    9. Dmitry V. Khoroshun,, Kurt Warncke,, Shyue-Chu Ke,, Djamaladdin G. Musaev, and, Keiji Morokuma. Internal Degrees of Freedom, Structural Motifs, and Conformational Energetics of the 5‘-Deoxyadenosyl Radical:  Implications for Function in Adenosylcobalamin-Dependent Enzymes. A Computational Study. Journal of the American Chemical Society 2003, 125 (2) , 570-579. https://doi.org/10.1021/ja028393k
    10. Antonio J. Pierik,, Daniele Ciceri,, Gerd Bröker,, Christopher H. Edwards,, William McFarlane,, Joachim Winter,, Wolfgang Buckel, and, Bernard T. Golding. Rotation of the exo-Methylene Group of (R)-3-Methylitaconate Catalyzed by Coenzyme B12-Dependent 2-Methyleneglutarate Mutase from Eubacterium barkeri. Journal of the American Chemical Society 2002, 124 (47) , 14039-14048. https://doi.org/10.1021/ja020340f
    11. Marija Semialjac and, Helmut Schwarz. Computational Exploration of Rearrangements Related to the Vitamin B12-Dependent Ethanolamine Ammonia Lyase Catalyzed Transformation. Journal of the American Chemical Society 2002, 124 (30) , 8974-8983. https://doi.org/10.1021/ja020101s
    12. Stacey D. Wetmore,, David M. Smith,, Bernard T. Golding, and, Leo Radom. Interconversion of (S)-Glutamate and (2S,3S)-3-Methylaspartate:  A Distinctive B12-Dependent Carbon-Skeleton Rearrangement. Journal of the American Chemical Society 2001, 123 (33) , 7963-7972. https://doi.org/10.1021/ja004246f
    13. Kathryn N. Rankin,, James W. Gauld, and, Russell J. Boyd. Hydrogen-Bond Mediated Catalysis:  The Aminolysis of 6-Chloropyrimidine as Catalyzed by Derivatives of Uracil. Journal of the American Chemical Society 2001, 123 (9) , 2047-2052. https://doi.org/10.1021/ja0038373
    14. L.K.Y. Cheung, A.D. Sanders, A.A. Houfani, D.A.S. Grahame, B.C. Bryksa, D.R. Dee, R.Y. Yada. Factors affecting enzyme activity and design. 2024, 17-57. https://doi.org/10.1016/B978-0-443-15437-9.00012-4
    15. Amarendra Nath Maity, Jun-Ru Chen, Quan-Yuan Li, Shyue-Chu Ke. The Nitrogen Atom of Vitamin B6 Is Essential for the Catalysis of Radical Aminomutases. International Journal of Molecular Sciences 2022, 23 (9) , 5210. https://doi.org/10.3390/ijms23095210
    16. Christof M. Jäger, Anna K. Croft. Radical Reaction Control in the AdoMet Radical Enzyme CDG Synthase (QueE): Consolidate, Destabilize, Accelerate. Chemistry – A European Journal 2017, 23 (4) , 953-962. https://doi.org/10.1002/chem.201604719
    17. Tobias Weinert, Simona G Huwiler, Johannes W Kung, Sina Weidenweber, Petra Hellwig, Hans-Joachim Stärk, Till Biskup, Stefan Weber, Julien J H Cotelesage, Graham N George, Ulrich Ermler, Matthias Boll. Structural basis of enzymatic benzene ring reduction. Nature Chemical Biology 2015, 11 (8) , 586-591. https://doi.org/10.1038/nchembio.1849
    18. Daniel P. Dowling, Anna K. Croft, Catherine L. Drennan. Radical Use of Rossmann and TIM Barrel Architectures for Controlling Coenzyme B 12 Chemistry. Annual Review of Biophysics 2012, 41 (1) , 403-427. https://doi.org/10.1146/annurev-biophys-050511-102225
    19. Caitlyn Makins, François N. Miros, Nigel S. Scrutton, Kirsten R. Wolthers. Role of histidine 225 in adenosylcobalamin-dependent ornithine 4,5-aminomutase. Bioorganic Chemistry 2012, 40 , 39-47. https://doi.org/10.1016/j.bioorg.2011.08.003
    20. Gregory M. Sandala, David M. Smith, Leo Radom. Theoretical Studies of Radical Enzymes. 2012https://doi.org/10.1002/9781119953678.rad051
    21. Bernhard Kräutler. Biochemistry of B12-Cofactors in Human Metabolism. 2012, 323-346. https://doi.org/10.1007/978-94-007-2199-9_17
    22. Perry Allen Frey. Cobalamin Coenzymes in Enzymology. 2010, 501-546. https://doi.org/10.1016/B978-008045382-8.00145-3
    23. Kirsten R. Wolthers, Stephen E.J. Rigby, Nigel S. Scrutton. Mechanism of Radical-based Catalysis in the Reaction Catalyzed by Adenosylcobalamin-dependent Ornithine 4,5-Aminomutase. Journal of Biological Chemistry 2008, 283 (50) , 34615-34625. https://doi.org/10.1074/jbc.M807911200
    24. Karmen Čondić‐Jurkić, V. Tamara Perchyonok, Hendrik Zipse, David M. Smith. On the modeling of arginine‐bound carboxylates: A case study with Pyruvate Formate‐Lyase. Journal of Computational Chemistry 2008, 29 (14) , 2425-2433. https://doi.org/10.1002/jcc.20984
    25. . Investigation of Fragmentation Patterns in Pyridoxal-primary Amine Complexes by Electrospray Ionization Mass Spectrometry. Bulletin of the Korean Chemical Society 2006, 947-950. https://doi.org/10.5012/bkcs.2006.27.6.947
    26. Wolfgang Buckel, Christoph Kratky, Bernard T. Golding. Stabilisation of Methylene Radicals by Cob( II )alamin in Coenzyme B 12 Dependent Mutases. Chemistry – A European Journal 2006, 12 (2) , 352-362. https://doi.org/10.1002/chem.200501074
    27. Ming-Jen Sheu, Shyue-Chu Ke. Molecular properties of the product radical in adenosylcobalamin-dependent ethanolamine deaminase. Physica A: Statistical Mechanics and its Applications 2005, 350 (1) , 131-143. https://doi.org/10.1016/j.physa.2004.11.028
    28. Matthias Boll. Key enzymes in the anaerobic aromatic metabolism catalysing Birch-like reductions. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2005, 1707 (1) , 34-50. https://doi.org/10.1016/j.bbabio.2004.01.009
    29. Marija Semialjac, Helmut Schwarz. Computational Investigation of Hydrogen Abstraction from 2‐Aminoethanol by the 1,5‐Dideoxyribose‐5‐yl Radical: A Model Study of a Reaction Occurring in the Active Site of Ethanolamine Ammonia Lyase. Chemistry – A European Journal 2004, 10 (11) , 2781-2788. https://doi.org/10.1002/chem.200305773
    30. Birgit Schiøtt. The influence of solvation on short strong hydrogen bonds: a density functional theory study of the Asp-His interaction in subtilisins. Chem. Commun. 2004, 26 (5) , 498-499. https://doi.org/10.1039/B314228K
    31. Ruma Banerjee, Stephen W. Ragsdale. The Many Faces of Vitamin B 12 : Catalysis by Cobalamin-Dependent Enzymes. Annual Review of Biochemistry 2003, 72 (1) , 209-247. https://doi.org/10.1146/annurev.biochem.72.121801.161828
    32. Karl Gruber, Christoph Kratky. Coenzyme B12 dependent glutamate mutase. Current Opinion in Chemical Biology 2002, 6 (5) , 598-603. https://doi.org/10.1016/S1367-5931(02)00368-X
    33. Stacey D. Wetmore, David M. Smith, Leo Radom. Catalysis by Mutants of Methylmalonyl-CoA Mutase: A Theoretical Rationalization for a Change in the Rate-Determining Step. ChemBioChem 2001, 2 (12) , 919-922. https://doi.org/10.1002/1439-7633(20011203)2:12<919::AID-CBIC919>3.0.CO;2-6
    34. David M. Smith, Stacey D. Wetmore, Leo Radom. Theoretical studies of coenzyme B12-dependent carbon-skeleton rearrangements. 2001, 183-214. https://doi.org/10.1016/S1380-7323(01)80006-6
    35. Kwang S. Kim, Kyung Seok Oh, Jin Yong Lee. Catalytic role of enzymes: Short strong H-bond-induced partial proton shuttles and charge redistributions. Proceedings of the National Academy of Sciences 2000, 97 (12) , 6373-6378. https://doi.org/10.1073/pnas.97.12.6373
    36. Meinrad Kunz, Jànos Rétey. Evidence for a 1,2 Shift of a Hydrogen Atom in a Radical Intermediate of the Methylmalonyl-CoA Mutase Reaction. Bioorganic Chemistry 2000, 28 (3) , 134-139. https://doi.org/10.1006/bioo.2000.1165
    37. Nilesh Maiti, Lusiana Widjaja, Ruma Banerjee. Proton Transfer from Histidine 244 May Facilitate the 1,2 Rearrangement Reaction in Coenzyme B12-dependent Methylmalonyl-CoA Mutase. Journal of Biological Chemistry 1999, 274 (46) , 32733-32737. https://doi.org/10.1074/jbc.274.46.32733
    38. Philip A. Butler, Bernhard Kräutler. Biological Organometallic Chemistry of B12. , 1-55. https://doi.org/10.1007/3418_004
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    Cite this: J. Am. Chem. Soc. 1999, 121, 6, 1383–1384
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja983512a
    Published January 30, 1999
    Copyright © 1999 American Chemical Society
    Request reuse permissions

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