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 x AIF4-, 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 beta-phosphate and AIF4- 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.
journal_name
Naturejournal_title
Natureauthors
Schindelin H,Kisker C,Schlessman JL,Howard JB,Rees DCdoi
10.1038/387370a0subject
Has Abstractpub_date
1997-05-22 00:00:00pages
370-6issue
6631eissn
0028-0836issn
1476-4687journal_volume
387pub_type
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