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

Schindelin, Hermann and Kisker, Caroline and Schlessman, Jamie L. and Howard, James B. and Rees, Douglas C. (1997) Structure of ADP·AIF_4 -stabilized nitrogenase complex and its implications for signal transduction. Nature, 387 (6631). pp. 370-376. ISSN 0028-0836. doi:10.1038/387370a0.

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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.

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Rees, Douglas C.0000-0003-4073-1185
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.
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Deutsche Forschungsgemeinschaft (DFG)UNSPECIFIED
Issue or Number:6631
Record Number:CaltechAUTHORS:20150617-132613769
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Official Citation:Structure of ADP·AIF4 –-stabilized nitrogenase complex and its implications for signal transduction 370 Hermann Schindelin, Caroline Kisker, Jamie L. Schlessman, James B. Howard & Douglas C. Rees doi:10.1038/387370a0
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:58326
Deposited By: Ruth Sustaita
Deposited On:17 Jun 2015 20:35
Last Modified:10 Nov 2021 22:03

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