Recent Progress in Research on the Structures and Functions of Nitrogenase Active Sites
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- Ohki Yasuhiro
- Department of Chemistry, Graduate School of Science, Nagoya University
Bibliographic Information
- Other Title
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- ニトロゲナーゼ活性中心の構造と機能に関する新展開
- ニトロゲナーゼ カッセイ チュウシン ノ コウゾウ ト キノウ ニ カンスル シン テンカイ
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Description
Nirtogenases are a class of enzymes that catalyze the reduction of N2 to NH3 under ambient conditions in the presence of protons and electrons. The active site of the most prevalent nitrogense is called as the FeMo-cofactor, which is often designated as the M-cluster. It consists of one molybdenum, seven irons, and several sulfur atoms, and represents the most complex metal-sulfur cluster in biology. Some homologues containing vanadium or iron in place of molybdenum exist in alternative nitrogenases, while a precursor of FeMo-cofactor was also identified as an all-iron homologue. Recent crystallographic and biochemical studies on nitrogenases uncovered some important clues about the structurefunction relationship of the nitrogenase active sites, such as the precise structure of the FeMo-cofactor, unique catalytic functions of the FeMo-cofactor and its homologues, and the detailedmechanistic insights in the nitrogen fixation. Transition-metal mediated conversion of small molecules that contain triple bonds has been of interest to the community of coordination chemistry, and this contribution introduces some important progresses in the nitrogenase chemistry/biochemistry made in recent years.
Journal
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- Bulletin of Japan Society of Coordination Chemistry
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Bulletin of Japan Society of Coordination Chemistry 66 (0), 26-30, 2015
Japan Society of Coordination Chemistry