Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

You’ve supercharged your research process with ACS and Mendeley!

STEP 1:
Click to create an ACS ID

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

MENDELEY PAIRING EXPIRED
Your Mendeley pairing has expired. Please reconnect
ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

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

View Author Information
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.
Cite this: J. Am. Chem. Soc. 1999, 121, 6, 1383–1384
Publication Date (Web):January 30, 1999
https://doi.org/10.1021/ja983512a
Copyright © 1999 American Chemical Society

    Article Views

    192

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

     Australian National University.

     University of Newcastle upon Tyne.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

    Cited By

    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