- 関
- iron-molybdenum cofactor、MoFe protein、molybdoferredoxin
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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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
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 ...
★リンクテーブル★
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- 英
- iron-molybdenum cofactor、FeMo cofactor
- 関
- モリブドフェレドキシン、モリブデン鉄タンパク質、鉄モリブデン補助因子
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- 関
- FeMo cofactor、MoFe protein、molybdoferredoxin
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- 関
- FeMo cofactor、iron-molybdenum cofactor、molybdoferredoxin
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モリブドフェレドキシン
- 関
- FeMo cofactor、iron-molybdenum cofactor、MoFe protein
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- 英
- [[]]
- 同
- FeMo cofactor
- 関
- [[]]
- 同
- FeMo cofactor
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鉄 iron sidero