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Title: 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
Keywords: Electron Transfer; Nitrogenase; Nitrogenase-like enzymes; DPOR
Issue Date: 2019
Publisher: Biochemical Journal
Abstract: 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.
Description: Tài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0
URI: http://dlib.hust.edu.vn/handle/HUST/24908
Link item primary: https://www.biorxiv.org/content/10.1101/840439v1
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường
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