ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

Determinants of Regioselectivity and Chemoselectivity in Fosfomycin Resistance Protein FosA from QM/MM Calculations

View Author Information
Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, D-45470, Mülheim an der Ruhr, Germany
Cite this: J. Phys. Chem. B 2013, 117, 5, 1326–1336
Publication Date (Web):January 15, 2013
https://doi.org/10.1021/jp4002719
Copyright © 2013 American Chemical Society

    Article Views

    664

    Altmetric

    -

    Citations

    12
    LEARN ABOUT THESE METRICS
    Other access options
    Supporting Info (1)»

    Abstract

    Abstract Image

    FosA is a manganese-dependent enzyme that utilizes a Mn2+ ion to catalyze the inactivation of the fosfomycin antibiotic by glutathione (GSH) addition. We report a theoretical study on the catalytic mechanism and the factors governing the regioselectivity and chemoselectivity of FosA. Density functional theory (DFT) calculations on the uncatalyzed reaction give high barriers and almost no regioselectivity even when adding two water molecules to assist the proton transfer. According to quantum mechanics/molecular mechanics (QM/MM) calculations on the full solvated protein, the enzyme-catalyzed glutathione addition reaction involves two major chemical steps that both proceed in the sextet state: proton transfer from the GSH thiol group to the Tyr39 anion and nucleophilic attack by the GSH thiolate leading to epoxide ring-opening. The second step is rate-limiting and is facilitated by the presence of the high-spin Mn2+ ion that functions as a Lewis acid and stabilizes the leaving oxyanion through direct coordination. The barrier for C1 attack is computed to be 8.9 kcal/mol lower than that for C2 attack, in agreement with the experimentally observed regioselectivity of the enzyme. Further QM/MM calculations on the alternative water attack predict a concerted mechanism for this reaction, where the deprotonation of water, nucleophilic attack, and epoxide ring-opening take place via the same transition state. The calculated barrier is 8.3 kcal/mol higher than that for GSH attack, in line with the observed chemoselectivity of the enzyme, which manages to catalyze the addition of GSH in the presence of water molecules around its active site. The catalytic efficiency, regioselectivity, and chemoselectivity of FosA are rationalized in terms of the influence of the active-site protein environment and the different stabilization of the distorted substrates in the relevant transition states.

    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.

    Supporting Information

    ARTICLE SECTIONS
    Jump To

    Setup of the systems; CHARMM parameters; IRC profiles and coordinates for the uncatalyzed reaction; active regions for QM/MM optimizations; QM, MM, and QM/MM energies for all stationary points; optimized structures for M2a (GSH attack) and M2b (water attack); complete citations for refs 42 , 53, and 55. This material is available free of charge via the Internet at http://pubs.acs.org.

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    This article is cited by 12 publications.

    1. Anderson H. Lima, José Rogério A. Silva, Cláudio Nahum Alves, Jerônimo Lameira. QM/MM Study of the Fosfomycin Resistance Mechanism Involving FosB Enzyme. ACS Omega 2021, 6 (19) , 12507-12512. https://doi.org/10.1021/acsomega.1c00096
    2. Lars Goerigk, Charles A. Collyer, and Jeffrey R. Reimers . Recommending Hartree–Fock Theory with London-Dispersion and Basis-Set-Superposition Corrections for the Optimization or Quantum Refinement of Protein Structures. The Journal of Physical Chemistry B 2014, 118 (50) , 14612-14626. https://doi.org/10.1021/jp510148h
    3. Zhe Li, Yinuo Wu, Ling-Jun Feng, Ruibo Wu, and Hai-Bin Luo . Ab Initio QM/MM Study Shows a Highly Dissociated SN2 Hydrolysis Mechanism for the cGMP-Specific Phosphodiesterase-5. Journal of Chemical Theory and Computation 2014, 10 (12) , 5448-5457. https://doi.org/10.1021/ct500761d
    4. Maja Lopandic, Fatima Merza, John F. Honek. Thermodynamic Overview of Bioconjugation Reactions Pertinent to Lysine and Cysteine Peptide and Protein Residues. Compounds 2023, 3 (3) , 464-503. https://doi.org/10.3390/compounds3030035
    5. Luiz P.C. Josino, Cláudio Nahum Alves, Anderson H. Lima. A molecular model to study FosA enzyme inhibition. Journal of Molecular Graphics and Modelling 2021, 107 , 107978. https://doi.org/10.1016/j.jmgm.2021.107978
    6. Paula Mihaljević-Jurič, Sérgio F. Sousa. A QM/MM Evaluation of the Missing Step in the Reduction Mechanism of HMG-CoA by Human HMG-CoA Reductase. Processes 2021, 9 (7) , 1085. https://doi.org/10.3390/pr9071085
    7. Wen-Jie Wei, Hui-Xia Qian, Wen-Juan Wang, Rong-Zhen Liao. Computational Understanding of the Selectivities in Metalloenzymes. Frontiers in Chemistry 2018, 6 https://doi.org/10.3389/fchem.2018.00638
    8. Andrea Novelli, Elia Rosi. Pharmacological properties of oral antibiotics for the treatment of uncomplicated urinary tract infections. Journal of Chemotherapy 2017, 29 (sup1) , 10-18. https://doi.org/10.1080/1120009X.2017.1380357
    9. Erik H. Klontz, Adam D. Tomich, Sebastian Günther, Justin A. Lemkul, Daniel Deredge, Zach Silverstein, JoAnna F. Shaw, Christi McElheny, Yohei Doi, Patrick L. Wintrode, Alexander D. MacKerell, Nicolas Sluis-Cremer, Eric J. Sundberg. Structure and Dynamics of FosA-Mediated Fosfomycin Resistance in Klebsiella pneumoniae and Escherichia coli. Antimicrobial Agents and Chemotherapy 2017, 61 (11) https://doi.org/10.1128/AAC.01572-17
    10. Cátia Moreira, Maria J. Ramos, Pedro Alexandrino Fernandes. Reaction Mechanism of Mycobacterium Tuberculosis Glutamine Synthetase Using Quantum Mechanics/Molecular Mechanics Calculations. Chemistry – A European Journal 2016, 22 (27) , 9218-9225. https://doi.org/10.1002/chem.201600305
    11. Eduardo F. Oliveira, Nuno M. F. S. A. Cerqueira, Maria J. Ramos, Pedro A. Fernandes. QM/MM study of the mechanism of reduction of 3-hydroxy-3-methylglutaryl coenzyme A catalyzed by human HMG-CoA reductase. Catalysis Science & Technology 2016, 6 (19) , 7172-7185. https://doi.org/10.1039/C6CY00356G
    12. Rong-Zhen Liao, Per E. M. Siegbahn. Mechanism and selectivity of the dinuclear iron benzoyl-coenzyme A epoxidase BoxB. Chemical Science 2015, 6 (5) , 2754-2764. https://doi.org/10.1039/C5SC00313J

    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