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  • 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.