Title
VTVH-MCD study of the Delta nifB Delta nifZ MoFe protein from Azotobacter vinelandii
Document Type
Article
Publication Date
4-8-2009
Abstract
NifZ is a member of a series of proteins associated with the maturation of the nitrogenase MoFe protein. An MCD spectroscopic study was undertaken on the Delta nifB Delta nifZ MoFe protein generated in the absence of both NifZ and NifB (deletion of NifB generates an apo-MoFe protein lacking the FeMo cofactor). Results presented here show that, in the absence of NifZ, only one of the two P-clusters of the MoFe protein is matured to the ultimate [8Fe-7S] structure. The other P-cluster site in the protein contains a [4Fe-4S] cluster pair, representing a P-cluster precursor that is electronically identical to the analogous clusters observed in the Delta nifH MoFe protein. These results suggest that the MoFe protein is synthesized in a stepwise fashion where NifZ is specifically required for the formation of the second P-cluster.
Publication Source (Journal or Book title)
Journal of the American Chemical Society
First Page
4558
Last Page
9
Recommended Citation
Cotton, M. S., Rupnik, K., Broach, R. B., Hu, Y., Fay, A. W., Ribbe, M. W., & Hales, B. J. (2009). VTVH-MCD study of the Delta nifB Delta nifZ MoFe protein from Azotobacter vinelandii. Journal of the American Chemical Society, 131 (13), 4558-9. https://doi.org/10.1021/ja807525m