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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Corless, Elliot | - |
| dc.contributor.author | Imran, Syed Muhammad Saad | - |
| dc.contributor.author | Watkins, Maxwell B | - |
| dc.date.accessioned | 2024-05-31T02:26:54Z | - |
| dc.date.available | 2024-05-31T02:26:54Z | - |
| dc.date.issued | 2019 | - |
| dc.identifier.other | OER000004058 | vi |
| dc.identifier.uri | http://dlib.hust.edu.vn/handle/HUST/24908 | - |
| dc.description | Tài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0 | vi |
| dc.description.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. | vi |
| dc.description.uri | https://www.biorxiv.org/content/10.1101/840439v1 | vi |
| dc.format | vi | |
| dc.language.iso | en | vi |
| dc.publisher | Biochemical Journal | vi |
| dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Vietnam | * |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/vn/ | * |
| dc.subject | Electron Transfer | vi |
| dc.subject | Nitrogenase | vi |
| dc.subject | Nitrogenase-like enzymes | vi |
| dc.subject | DPOR | vi |
| dc.subject.lcc | QD405 | vi |
| dc.title | The flexible N-terminus of BchL protects its [4Fe-4S] cluster in oxygenic environments and autoinhibits activity | vi |
| dc.type | Journal article | vi |
| Appears in Collections: | OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường | |
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