Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.
作者： D Wolle , D. Dean , J. Howard
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摘要: Electron transfer in nitrogenase involves a gating process initiated by MgATP (magnesium adenosine triphosphate) binding to Fe-protein. The redox site, an 4Fe:4S cluster, is structurally separated from the site. For hydrolysis be coupled electron transfer, signal transduction mechanism proposed that similar guanosine triphosphatase proteins. Based on three-dimensional structure of Fe-protein, Asp125 likely part putative path. Altered Fe-protein with Glu replacing Asp has been prepared and retains ability for initial nucleotide-dependent conformational change. However, either MgADP or can induce shift Mg nucleotide no longer essential.
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