Current Nanoscience

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Electron Transfer and Nano-Scale Motions in Nitrogenase Fe-Protein

Author(s): Mi Suk Jeong, Se Bok Jang.

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.

Keywords: Fe-protein, [FeS] metal cluster, Nucleotide, Conformational changes, Signal transduction, Electron transfer

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Article Details

VOLUME: 2
ISSUE: 1
Year: 2006
Page: [33 - 41]
Pages: 9
DOI: 10.2174/157341306775473773