Analysis of active sites for N2 and H+ reduction on FeMo-cofactor of nitrogenase

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• 作者：Feng Guan (1)
  DeHua Zhao (1)
  Miao Pan (1)
  Wei Jiang (1)
  Jilun Li (1)
  
• 关键词：Azotobacter vinelandii mutants ; nitrogenase ; dinitrogen and proton reduction sites ; electron transfer pathways
• 刊名：Chinese Science Bulletin
• 出版年：2007
• 出版时间：August 2007
• 年：2007
• 卷：52
• 期：15
• 页码：2088-2094
• 全文大小：1221KB
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• 作者单位：Feng Guan (1)
  DeHua Zhao (1)
  Miao Pan (1)
  Wei Jiang (1)
  Jilun Li (1)
  
  1. State Key Laboratory for Agrobiotechnology and Department of Microbiology & Immunology, China Agricultural University, Beijing, 100094, China
  
• ISSN：1861-9541

文摘

Dinitrogen (N2) and proton (H+), which act as physiological substrates of nitrogenase, are reduced on FeMo-co of the MoFe protein. However, researchers have different opinions about their exact reduction sites. Nitrogenases were purified from the wild type (WT) and five mutants of Azotobacter vinelandii (Av), including Qα191K, Hα195Q, nifV ?/sup>, Qα191K/nifV ?/sup> Hα195Q/nifV ?/sup>; and the activities of these enzymes for N2 and H+ reduction were analyzed. Our results suggest that the Fe2 and Fe6, atoms closed to the central sulfur atom (S2B) within FeMo-co, are sites for N2 binding and reduction and the Mo atom of FeMo-co is the site for H+ reduction. Combining these data with further bioinformatical analysis, we propose that two parallel electron channels may exist between the [8Fe7S] cluster and FeMo-co.