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Published May 22, 1997 | public
Journal Article

Structure of ADP·AIF_4 -stabilized nitrogenase complex and its implications for signal transduction

Abstract

The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP·AIF_4 –, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The β-phosphate and AIF_4 – groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.

Additional Information

© 1997 Nature Publishing Group. Received 5 December 1996; accepted 26 March 1997. Supported by the NIH (D.C.R. and J.B.H.), the NSF (J.B.H.) and by Deutsche Forschungsgemeinschaft postdoctoral fellowships (to C.K. and H.S.). X-PLOR calculations were performed on the CRAY C90 at the San Diego Supercomputer Center, supported by the NSF.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023