Atomic description of an enzyme reaction dominated by proton tunneling

Laura Masgrau, Anna Roujeinikova, Linus O. Johannissen, Parvinder Hothi, Jaswir Basran, Kara E. Ranaghan, Adrian J. Mulholland, Michael J. Sutcliffe, Nigel S. Scrutton, David Leys

    Research output: Contribution to journalArticlepeer-review


    We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at near-atomic resolution, we have identified the reaction pathway for tryptamine oxidation by aromatic amine dehydrogenase. Combining experiment and computer simulation, we show proton transfer occurs predominantly to oxygen O2 of Asp128β in a reaction dominated by tunneling over ∼0.6 angstroms. The role of long-range coupled motions in promoting tunneling is controversial. We show that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required.
    Original languageEnglish
    Pages (from-to)237-241
    Number of pages4
    Issue number5771
    Publication statusPublished - 14 Apr 2006


    • Alcaligenes faecalis/*enzymology
    • Aspartic Acid/chemistry
    • Binding Sites
    • Catalysis
    • Chemistry, Physical
    • Computer Simulation
    • Crystallography, X-Ray
    • Kinetics
    • Models, Chemical
    • Motion
    • Oxidation-Reduction
    • Oxidoreductases Acting on CH-NH Group Donors/*chemistry/*metabolism
    • Oxygen/chemistry
    • *Protons
    • Research Support, Non-U.S. Gov't
    • Temperature
    • Thermodynamics
    • Tryptamines/*metabolism
    • Water/chemistry


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