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Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii

Nature volume 360, pages 553–560 (1992)Cite this article

Abstract

The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7 Å resolution. The α- and β-subunits in this α2 β2 tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the α-subunit, whereas the P-cluster pair occurs at the interface between α- and β-subunits. Structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre

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Author notes

  1. D. C. Rees: To whom correspondence should be addressed.

Authors and Affiliations

  1. Division of Chemistry and Chemical Engineering 147-75CH, California Institute of Technology, Pasadena, California, 91125, USA

    Jongsun Kirn & D. C. Rees

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  1. Jongsun Kirn
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  2. D. C. Rees
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Kirn, J., Rees, D. Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii. Nature 360, 553–560 (1992). https://doi.org/10.1038/360553a0

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