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Showing 1–4 of 4 results
Advanced filters: Author: Jahaun Azadmanesh Clear advanced filters

  • The activity of human manganese superoxide dismutase (MnSOD) is determined by the state of a key catalytic residue, Tyr34, which was reported to undergo cyclic deprotonation and protonation events to promote the electron transfers of MnSOD. Here, the authors performed neutron diffraction, X-ray spectroscopy, and quantum chemistry calculations of Tyr34Phe MnSOD in oxidized, reduced and product inhibited enzymatic states, to elucidate the role of Tyr34 in MnSOD catalysis.

    • Jahaun Azadmanesh
    • Katelyn Slobodnik
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-17

  • Human manganese superoxide dismutase is an oxidoreductase that converts superoxide to molecular oxygen and hydrogen peroxide with proton-coupled electron transfers (PCETs), and has evolved to be highly product inhibited to limit the formation of hydrogen peroxide. Here, the authors use neutron diffraction and X-ray absorption spectroscopy of the product-bound, trivalent, and divalent states of the enzyme to identify the product-inhibited complex and propose a PCET mechanism.

    • Jahaun Azadmanesh
    • Katelyn Slobodnik
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Human manganese superoxide dismutase (MnSOD) is an oxidoreductase that uses concerted proton and electron transfers to reduce the levels of superoxide radicals in mitochondria, but mechanistic insights into this process are limited. Here, the authors report neutron crystal structures of Mn3+SOD and Mn2+SOD, revealing changes in the protonation states of key residues in the enzyme active site during the redox cycle.

    • Jahaun Azadmanesh
    • William E. Lutz
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12