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Abstract

The 3D crystallographic structure of the nitrogenase MoFe protein was first determined for the protein from Azotobacter vinelandii (Av1) at 2.8 Å resolution and identified two unique metal-sulphur clusters viz the FeMoco centres and the P clusters (Kim, Rees 1992). This structure was later refined to 2.2 Å resolution (Chan et al, 1993). Analysis of the structure of the MoFe protein from Clostridium pasteurianum (Cpl) was consistent with the formulation of FeMoco as MoFe7S9. homocitrate but differed in the interpretation of the structure of the P clusters (Bolin et al, 1993). Rees’s group reported that the P clusters consisted of two Fe4S4 clusters bonded through a disulphide bridge at one corner whereas Bolin suggested that the two Fe4S4 cubanes shared a single sulphur atom at the corner to produce an Fe8S7 cluster. (Fig 1)

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© 1998 Springer Science+Business Media Dordrecht

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Smith, B.E. et al. (1998). Structure of Klebsiella pneumoniae Nitrogenase. In: Elmerich, C., Kondorosi, A., Newton, W.E. (eds) Biological Nitrogen Fixation for the 21st Century. Current Plant Science and Biotechnology in Agriculture, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5159-7_9

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  • DOI: https://doi.org/10.1007/978-94-011-5159-7_9

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6169-8

  • Online ISBN: 978-94-011-5159-7

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