WordNet
- a substance (as a coenzyme) that must join with another to produce a given result
PrepTutorEJDIC
- ironの化学記号
UpToDate Contents
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- 1. 血管内皮機能および血栓溶解療法の基本的メカニズム vascular endothelial function and fundamental mechanisms of fibrinolysis thrombolysis
- 2. 静脈血栓症の原因の概要 overview of the causes of venous thrombosis
- 3. アンチトロンビン（ATIII）欠乏症 antithrombin atiii deficiency
- 4. 補体系の制御因子および受容体 regulators and receptors of the complement system
- 5. 静脈血栓症が確認された患者の評価 evaluation of the patient with established venous thrombosis
English Journal
- A journey into the active center of nitrogenase.
- Hu Y1, Ribbe MW.
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry.J Biol Inorg Chem.2014 Aug;19(6):731-6. doi: 10.1007/s00775-014-1137-2. Epub 2014 Apr 22.
- Nitrogenase catalyzes the reduction of N2 to NH3, a key step in the global nitrogen cycle. This article describes our journey toward the definition of a complete molecular structure of the active site of nitrogenase, with an emphasis on the discovery of the interstitial carbide and the radical SAM-d
- PMID 24752864
- Nitrogenase FeMo cofactor: an atomic structure in three simple steps.
- Einsle O.
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry.J Biol Inorg Chem.2014 Aug;19(6):737-45. doi: 10.1007/s00775-014-1116-7. Epub 2014 Feb 21.
- The enzyme nitrogenase catalyzes the six-electron reduction of molecular dinitrogen to ammonium, concomitant with the reduction of protons to yield hydrogen gas. In the MoFe protein component of the nitrogenase system, the unique FeMo cofactor is the active site of catalysis, but its exact mechanism
- PMID 24557709
- Substrate channel in nitrogenase revealed by a molecular dynamics approach.
- Smith D1, Danyal K, Raugei S, Seefeldt LC.
- Biochemistry.Biochemistry.2014 Apr 15;53(14):2278-85. doi: 10.1021/bi401313j. Epub 2014 Apr 2.
- Mo-dependent nitrogenase catalyzes the biological reduction of N2 to two NH3 molecules at FeMo-cofactor buried deep inside the MoFe protein. Access of substrates, such as N2, to the active site is likely restricted by the surrounding protein, requiring substrate channels that lead from the surface t
- PMID 24654842
Japanese Journal
- クロロフィル生合成系酵素と窒素固定酵素の共通構造基盤
- 村木 則文,栗栖 源嗣,野亦 次郎 [他],藤田 祐一
- 日本結晶学会誌 53(2), 113-118, 2011-04-30
- … The spatial arrangement of the NB-cluster and Pchlide is almost identical to that of the P-cluster and FeMo-cofactor in nitrogenase NifDK, suggesting that a common architecture exists to reduce chemically stable multibonds of porphyrin and dinitrogen. …
- NAID 10028253933
- ニトロゲナーゼおよび[NiFe]ヒドロゲナーゼ活性部位の人工構築
- 大木 靖弘,巽 和行
- 觸媒 = Catalyst 51(8), 570-576, 2009-12-10
- NAID 10026054968
- ニトロゲナーゼ活性部位とそのモデル
- 溝部 裕司
- 触媒 = Catalysts & Catalysis 46(4), 293-298, 2004-06-10
- NAID 10013450123
Related Links
- The FeMo-cofactor has been printed several times now, with very nice results. I print it with a raft, so it may be separated easily from the base. It does not need any supports, as I have added the supports in tinkercad. I have included ...
- The enzyme nitrogenase is the only known biological system able to break the triple bond of dinitrogen to yield bioavailable ammonium (1). Its active site, the FeMo cofactor, is a [Mo:7Fe:9S:X]:homocitrate cluster, the largest and ...
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★リンクテーブル★
| リンク元 | 「鉄モリブデン補酵素」「iron-molybdenum cofactor」「MoFe protein」「molybdoferredoxin」「FeMo補因子」 |
| 関連記事 | 「Fe」 |
「鉄モリブデン補酵素」
「iron-molybdenum cofactor」
「MoFe protein」
「molybdoferredoxin」
「FeMo補因子」
- 英
- [[]]
- 同
- FeMo cofactor
- 関
- [[]]