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2000
Volume 2, Issue 1
  • ISSN: 1573-4137
  • E-ISSN: 1875-6786

Abstract

During biological nitrogen fixation, the nitrogenase Fe-protein containing the [4Fe-4S] metal cluster has been shown to function in electron transfer to the MoFe-protein. This function of the Fe-protein is dependent on its conformational state and the metal cluster of the active site. This review will summarize the structures of the nucleotide bound (or "off") and amino-acid-substituted Fe-protein as well as the properties of the metal cluster in Fe-protein. The conformational changes in the nucleotide-dependent switch regions increase the driving force, leading to intermolecular electron transfer and macromolecular complex formation from the [4Fe-4S] metal cluster of the Fe-protein to the substrate reduction site of the MoFe-protein.

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/content/journals/cnano/10.2174/157341306775473773
2006-02-01
2024-11-02
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