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  • OER000002697.pdf.jpg
  • Journal article

  • CryoEM Structures of the Nitrogenase Complex During Catalytic Turnover

    • Authors : Rutledge, Hannah L. (2023)

  • The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multi-electron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here we report the cryogenic electron microscopic interrogation of the nitrogenase complex under enzymatic ...
  • OER000000768.pdf.jpg
  • Journal article

  • Substrate sensing institutes sequential and asymmetric electron transfer in the nitrogenase-like DPOR complex

    • Authors : Corless, Elliot I; Bennett, Brian; Antony, Edwin (2020)

  • Dark-operative protochlorophyllide oxidoreductase (DPOR) catalyzes the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide), a key penultimate step in the biosynthesis of bacteriochlorophyll. DPOR shares structural homology with nitrogenase and is made of electron donor (BchL) and electron acceptor (BchNB) component proteins. ATP driven assembly of the BchL and BchNB proteins drives electron transfer and Pchlide reduction. BchNB is composed of two subunits each&...
  • OER000004058.pdf.jpg
  • Journal article

  • The flexible N-terminus of BchL protects its [4Fe-4S] cluster in oxygenic environments and autoinhibits activity

    • Authors : Corless, Elliot; Imran, Syed Muhammad Saad; Watkins, Maxwell B (2019)

  • It is propose that ATP-binding produces a conformational compaction of the BchL homodimer leading to a release of the flexible N-terminus from blocking the [4Fe-4S] cluster and promotes complex formation with BchNB to drive electron transfer. The auto-inhibitive feature and release mechanism appear unique to DPOR and is not found in the structurally similar nitrogenase.